Showing papers on "Esterase published in 1970"
TL;DR: The observed distribution of the three most common bands fits the hypothesis that they are controlled by a set of autosomal alleles, and evidence for the genetic control of the fastest migrating set was obtained from population genetic analyses.
Abstract: The esterase enzymes of the tissues of Atlantic herring (Clupea harengus harengus) were analyzed by starch gel electrophoresis. Four sets of esterase bands were distinguished by their electrophoretic mobility, their relative activity with the two substrates, alpha-naphthyl acetate and alpha-naphthyl butyrate, and their relative concentrations in plasma, liver, and heart tissues. All of the esterases were inhibited by 10−4M solutions of dichlorvos, an organophosphate inhibitor, but none was inhibited by 10−4M eserine sulfate or by 10−4 M EDTA. Polymorphism was noted in all four sets of esterases. Evidence for the genetic control of the fastest migrating set was obtained from population genetic analyses. In this set of esterases, five distinct bands occurred either singly or in pairs. The observed distribution of the three most common bands fits the hypothesis that they are controlled by a set of autosomal alleles. The two rarest bands occurred only in the heterozygous state, as would be expected. ...
633 citations
TL;DR: Findings will contribute to a more complete phenotypic characterization of those mutants of sporulation that appear to be involved in the production of extracellular hydrolytic enzymes.
Abstract: Summary. This study has characterized 3 proteolytic enzymes during sporulation by Bacillus subtilis Marburg strain when grown in nutrient broth. A method of purification is described which permits the separation of 2 different proteinases: one belonging to the metal enzyme group and the other to the serine enzyme group. The third enzyme, probably an esterase, showed a high esterolytic activity, but only low proteolytic activity. Determination of the 3 enzymes in a mixture was accomplished by using specific substrates and inhibitors. They were excreted simultaneously between the end of the growth phase until the appearance of the prespores. During this entire period, 20% of the total proteolytic activity was due to the metal proteinase; 80% of the proteolytic activity and 15% of the esterolytic activity was due to the serine proteinase; 85% of the esterolytic activity was the result of the esterase. These findings will contribute to a more complete phenotypic characterization of those mutants of sporulation that appear to be involved in the production of extracellular hydrolytic enzymes.
192 citations
TL;DR: The studies suggest that the α2-macroglobulin is a major plasma inhibitor of kallikrein and provide a new example of an interrelationship between the coagulation, fibrinolytic, and kall Kikrein enzyme systems.
Abstract: Activation of plasma kallikrein arginine esterase activity by kaolin resulted in peak activity at 1 min of incubation and a 50% reduction in activity at 5 min in normal plasma, and 30% reduction in the plasma of patients with hereditary angioneurotic edema who lacked the C1 inactivator. The peak esterolytic activity was inhibited by soybean trypsin inhibitor whereas the 5 min activity was resistant to this inhibitor. Acid treatment of normal and hereditary angioneurotic edema plasma destroyed the factor responsible for the fall in esterase activity at 5 min and the factor which rendered the esterase resistant to soybean trypsin inhibitor. Purified alpha(2)-macroglobulin inhibited approximately 50% of the TAMe esterase activity of purified plasma kallikrein without changing its activity toward basic amino acid esters. The interaction between the alpha(2)-macroglobulin and kallikrein resulted in alterations in the gel filtration chromatographic pattern of the TAMe esterase and biologic activity of kallikrein, indicating that kallikrein was bound to the alpha(2)-macroglobulin. The TAMe esterase activity of this complex, isolated by column chromatography, was resistant to C1 inactivator and SBTI. Studies of incubation mixtures of kallikrein, alpha(2)-macroglobulin and C1 inactivator suggested that these inhibitors compete for the enzyme, and that the alpha(2)-macroglobulin partially protects the esterase activity of kallikrein from C1 inactivator. The alpha(2)-macroglobulin isolated from kaolin-activated plasma possessed 240 times the esterolytic activity of the alpha(2)-macroglobulin purified from plasma treated with inhibitors of kallikrein and of its activation. The alpha(2)-macroglobulin blocked the uterine-containing activity and vascular permeability-inducing effects of plasma kallikrein. These studies suggest that the alpha(2)-macroglobulin is a major plasma inhibitor of kallikrein and provide a new example of an interrelationship between the coagulation, fibrinolytic, and kallikrein enzyme systems.
142 citations
TL;DR: The proposed regulator element involved is probably structurally linked to C(10); however, linkage to a member of the D or G groups cannot be completely excluded.
Abstract: The ES-2 esterase is a kidney-associated esterase and is expressed in a cloned mouse renal adenocarcinoma cell line. Somatic cell hybridization of the mouse renal adenocarcinoma with either mouse or human fibroblasts leads to the marked reduction of ES-2 esterase titer. The extinction of ES-2 esterase activity in mouse×human hybrids is reversible. Extinction correlates with the presence of the human C10 chromosome in the somatic cell hybrids; whereas reexpression of the ES-2 esterase is observed in hybrids which have lost C10. Thus, the proposed regulator element involved is probably structurally linked to C10; however, linkage to a member of the D or G groups cannot be completely excluded.
90 citations
TL;DR: The ontogeny of the esterase isozymes of the teleost, Fundulus heteroclitus, has been investigated and there appear to be at least 15 different esterases, which constitute 6–8 groups, each of which is probably encoded in one or more genetic loci.
Abstract: The ontogeny of the esterase isozymes of the teleost, Fundulus heteroclitus, has been investigated. One group of esterase isozymes is present at all stages of development, whereas other esterase isozymes only very gradually appear at later stages of development, or abruptly appear at such dramatic developmental events as hatching. The ontogeny of these isozyme patterns is interpreted as the expression of differential regulation of separate esterase genes. The general pattern of teleost esterase gene activation is similar to that reported for birds and mammals. Allelic variation was detected at two of the esterase loci. On the basis of electrophoretic mobility, substrate specificity, inhibitor specificity, genetic variation, and ontogeny of esterases, there appear to be at least 15 different esterase isozymes, which constitute 6–8 groups, each of which is probably encoded in one or more genetic loci.
73 citations
TL;DR: An enzyme in extracts of luteinized rat ovaries was found which catalyzed the synthesis of cholesterol esters from palmitic acid-l-14C and cholesterol and required ATP, Mg++ and Coenzyme A for expression of activity.
Abstract: An enzyme in extracts of luteinized rat ovaries was found which catalyzed the synthesis of cholesterol esters from palmitic acid-l-14C and cholesterol and required ATP, Mg++ and Coenzyme A for expression of activity. This enzyme, sterol acyl transferase, was associated predominantly with the 100,000 ×g pellet fraction obtained from 10,000 ×g supernatant fractions of homogenized ovaries. The enzyme which hydrolyzes cholesterol esters, sterol esterase, was assayed simultaneously in 100,000 ×g supernatant fractions. Transferase and esterase levels were both markedly reduced (p <.01) when assayed 3 days after hypophysectomy (90 and 70%, respectively). Administration of rat prolactin (2 IU; sc; b.i.d.) was completely effective in preventing the decline of both enzymes after hypophysectomy, whereas LH (NIH-LH-S14; 50 μg daily in sesame oil+5% beeswax) was without effect. In hypophysectomized animals, LH and prolactin combined were less effective in maintaining transferase activity than prolactin treatment alone...
71 citations
Journal Article•
TL;DR: Direct biochemical evidence is provided that the rabbit blood neutrophil contains a precursor esterase involved in the cell response to the chemotactic stimulus C567, and that contact of the cell withChemotactic factor leads to activation of the proesterase.
Abstract: Direct biochemical evidence is provided that the rabbit blood neutrophil contains a precursor esterase involved in the cell response to the chemotactic stimulus C567, and that contact of the cell with chemotactic factor leads to activation of the proesterase. Rabbit blood leukocytes contain esterase 1, that is, an enzyme capable of hydrolyzing acetyl-dl-phenylalanine β-naphthyl ester. This activity can be ascribed largely, if not entirely, to the presence of neutrophils. Comparing blood leukocytes with peritoneal (exudate) neutrophils, the former cells contain greater esterase activity as well as greater chemotactic responsiveness. Treatment of blood leukocytes, but not peritoneal neutrophils, with chemotactic factor results in the acquisition of esterase activity (“esterase activation”) and chemotactic deactivation (loss of chemotactic responsiveness). By using highly purified complement and preparative (density gradient) ultracentrifugation, and employing agents that dissociate the macromolecular chemotactic factor, the phenomena of chemotactic activity, esterase-activating capacity and deactivating potential have been shown to be interrelated and clearly ascribable to C567. The esterase that appears in the blood leukocyte as a result of interaction with C567 can be identified as esterase 1, on the basis of exquisite sensitivity to inhibitory effects of phosphonate compounds at very low concentrations (10-8 M). These data provide direct biochemical support for the original hypothesis that the chemotactic response of the neutrophil to the complement chemotactic factor C567 involves an interaction which results in the conversion of the cell-bound proesterase to an active esterase. The biochemical role of this esterase in the kinetic behavior of the granulocyte is not known. This information may have special relevance to at least four other phenomena in which activation of a protesterase to an active esterase as the cause of an “allergic response” has been postulated on the basis of indirect evidence.
69 citations
TL;DR: The resemblances between zymograms of the species examined agree with the affinities based on cytogenetic analyses, and the potential usefulness of this information for taxonomic and evolutionary studies is indicated.
58 citations
TL;DR: The effects of photooxidation produced a permanent change in the enzyme whereas the dark inhibitions were completely reversed by removal of the dye from the enzyme surface with charcoal treatment.
57 citations
TL;DR: Electrophoretic separation is described for acid phosphatase, non-specific esterase, leucine amino peptidase, lactase, malate, α-glutamate, glucose-6-ph phosphate and 6-phosphogluconate dehydrogenases from adults of four populations of Schistosoma mansoni and one population of S. haematobium, finding clear qualitative differences between species.
52 citations
TL;DR: It is indicated that the esterase and the lyase from Clostridium multifermentans were either complexed or similar molecular species and both activities were most stable at pH 6.0.
Abstract: Exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans were purified 156-fold and 178-fold, respectively, by gel filtration chromatography on Sephadex G-200. The activities of both enzymes coincided in a single protein peak. Profiles of the two activities also coincided in diethylaminoethyl-cellulose chromatography and zonal centrifugation. These studies indicated that the esterase and the lyase were either complexed or similar molecular species. The former seems more probable because of the relatively high molecular weight. Both activities were most stable at pH 6.0. The esterase was inactivated rapidly at pH 5 or 7. Lyase preparations were freed of pectinesterase activity by heating for 30 min at 38 C and pH 7.0.
TL;DR: By means of cytochemical investigations on 140 cases of various hemoblastoses a so-called naphthol AS-D chloroacetate esterase defect could be detected in a considerable number of the myeloid cases, which suggests a myeloids rather than a lymphatic disease of the blood forming system.
Abstract: Some observations with the naphthol AS-D chloroacetate esterase reaction are reported and their diagnostic significance is discussed. This is illustrated by some characteristic cases. By means of cytochemical investigations on 140 cases of various hemoblastoses a so-called naphthol AS-D chloroacetate esterase defect could be detected in a considerable number of the myeloid cases. Therefore, the demonstration of such an enzyme defect in diagnostic doubtful cases suggests a myeloid rather than a lymphatic disease of the blood forming system. The occurence of pseudo-Pelger cells can be interpreted in the same sense, as they sometimes contain naphthol AS-D chloroacetate esterase positive Auer rods, which proves their neoplastic nature in such cases. Furthermore, very immature hemoblastoses can be identified as myeloid, if only few of the blasts reveal a positive naphthol AS-D chloroacetate esterase reaction. Finally it is mentioned that in rare cases, contrary to their normal behaviour, cosinophils may present with a positive naphthol AS-chloroacetate esterase reaction.
TL;DR: Starch gel electrophoresis of sonicated rabbit red cells using a modified system of buffers gave a maximum of 24 zones of esterase activity with α-naphthyl acetate as substrate, and 17 of the zones common to gels developed with any of these substrates were divided into three systems of isozymes.
Abstract: Starch gel electrophoresis of sonicated rabbit red cells using a modified system of buffers gave a maximum of 24 zones of esterase activity with α-naphthyl acetate as substrate, 23 with α-naphthyl propionate, and 20 with α-naphthyl butyrate. Seventeen of the zones common to gels developed with any of these substrates were divided into three systems of isozymes, one of which, genetic system 1, has been previously described by Grunder et al. (1965). The zones of system 2 migrated between those of system 1 and those of system 3, the most anodal system. Each of these new systems, like system 1, consisted of three phenotypes controlled, respectively, by a pair of codominant autosomal alleles. In 10 test-cross matings involving systems 1 and 2, not more than two of four possible phenotypes were observed in the offspring of each family, thereby indicating close linkage of the two loci. Based on those matings, the probability that the two loci are independent was less than 0.0001.
TL;DR: Modification of carboxypeptidase A with 1-cyclohexyl-3-(2-morpholinoethyl)-carbodiimide metho-p-toluene sulfonate at pH 6.0 simultaneously abolishes both esterase and peptidase activities.
TL;DR: The results suggest that at least five contiguous peptide units of the substrate can interact concurrently with the enzyme, and the increased effectiveness of the enzyme with larger substrates appears mainly in the acylation reaction and, to a lesser extent, in the binding and deacylation steps.
Abstract: Large increases in the esterase, amidase, and peptidase activities of elastase are observed on increasing the length of peptide substrates. The results suggest that at least five contiguous peptide units of the substrate (four N-terminal and one C-terminal to the scissile bond) can interact concurrently with the enzyme. When analyzed in terms of an acyl-enzyme mechanism, the increased effectiveness of the enzyme with larger substrates appears mainly in the acylation reaction and, to a lesser extent, in the binding and deacylation steps.
TL;DR: The α-Galactosidase (α- d -galactoside galactohydrolase, EC 3.23) and β-galactosaidase were extracted from spinach leaves and separated from each other by chromatography on DEAE-cellulose and by Sephadex gel filtration.
TL;DR: An intracellular glycerol ester hydrolase (lipase) from Propionibacterium shermanii was recovered from cell-free extracts and purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography on diethylaminoethylcellulose.
Abstract: An intracellular glycerol ester hydrolase (lipase) from Propionibacterium shermanii was recovered from cell-free extracts and purified by ammonium sulfate precipitation, gel filtration, and ion-exchange chromatography on diethylaminoethylcellulose. Maximum enzyme activity was observed at pH 7.2 and 47 C when an emulsion of tributyrin was used as substrate. The enzyme was stable between pH 5.5 and 8. Heating the enzyme solution at 45 C for 10 min resulted in a 75% decrease in activity. Maximum rate of hydrolysis of triglycerides was observed on tripropionin, followed in order by tributyrin, tricaproin, and tricaprylin. The lipase was strongly inhibited by mercury and arsenicals, but specific sulfhydryl reagents had little or no inhibiting effect on the enzyme activity. The enzyme also showed some esterase activity, but the hydrolysis of substrates in solution was small as compared to the hydrolysis of substrates in emulsion.
TL;DR: UDPase, esterase, and 5′-nucleotidase were measured as a function of cell cycle time in L5178Y cells synchronized with excess thymidine and colcemid and each enzyme followed a peak pattern.
TL;DR: The remarkable correspondance between theperiod of reduced esterase activity in the crypt and the period of increased proliferative activity after various radiation doses suggest a relationship between changes in crypt cell population dynamics and ester enzyme activity.
Abstract: The effect of low doses of x-irradiation (50-400 R)on the activity of various enzymes in rat intestinal epithehiuni has been investigated by histochemical staining methods and quantitative microchemical analyses of crypts and villi dissected from frozen-dried sections. Irradiation had no effect on the activities of enzymes which in nonirradiated animals are present exclusively or mainly in the villus epithehium (aminopeptidase, various phosphatases) or are evenly distributed along the epithelium of crypts and villi (various dehydrogenases). However, nonspecific esterase activity decreased markedly both in crypt epithehum and vihlus epithelium. This occurred 36 hr after irradiation, independent of the radiation dose. The number of crypt cells with reduced esterase activity and the duration of the effect increased with higher radiation doses. These results were confirmed by quantitative analyses which also showed that esterase activity is 5 times higher in the villus than in the crypt. The remarkable correspondance between the period of reduced esterase activity in the crypt and the period of increased proliferative activity after various radiation doses suggest a relationship between changes in crypt cell population dynamics and esterase activity; the functional consequences for the villus epithelium of changes in the crypt cells afterirradiation are discussed.
TL;DR: Esterase and profile changes may reflect a role of lipids in sporulation and physiological ageing, and intracellular lipid decreased with increase in esterase activity function.
Abstract: SUMMARY: Esterases, determined by polyacrylamide gel electrophoresis, were present when Candida lipolytica was grown in a liquid, shaken, glucose-mineral salts medium. Intracellular esterase activity increased during growth, but extracellular esterase activity was small and increased only marginally. Esterases were not detected in organisms grown on solid glucose-mineral salts medium, but were present when glycerol tributyrin replaced glucose.
At the onset of asexual sporulation in a yeast-like fungus, three new esterases occurred. Intracellular esterase activity increased, intracellular lipid utilization occurred, and the respiratory quotient decreased. No extracellular esterase activity was detected.
Esterases were only detected in Aspergillus niger at late stages of conidiation when intracellular lipid decreased. Esterase activity was not detected in the mitochondria or in the cell-free growth medium.
Esterases of all organisms tested hydrolysed glycerol tributyrin and were arbitrarily classified as lipases; intracellular lipid decreased with increase in esterase activity function. Esterase and profile changes may reflect a role of lipids in sporulation and physiological ageing.
TL;DR: It is demonstrated that the enzyme deficiency is not complete in all cases and that certain of the sera which contain trace amounts of enzyme activity differ with respect to their immunological reactions and their electrophoretic esterase pattern.
Abstract: The serum enzyme pseudocholinesterase from 14 individuals of the rare phenotype S (silent gene) has been investigated by means of various biochemical and immunological techniques. By use of more sensitive methods than standard assays, it is demonstrated that the enzyme deficiency is not complete in all cases and that certain of the sera which contain trace amounts of enzyme activity differ with respect to their immunological reactions and their electrophoretic esterase pattern.
30 Apr 1970
TL;DR: Specific activities of LDH and esterase decreased during lag, remained low during log, and then rose to original levels during plateau phase of growth in PK in vitro cell populations, suggesting that cellular topology may importantly influence the activities of unrelated enzymes.
TL;DR: In this article, a correlation was found between biochemically determined hydroxylations and enzymhisto-chemically determined NADPH-nitro-BT reductase and Naphthol-AS-D esterase.
Abstract: Male and female rat liver were studied during post-natal development. A correlation was found between biochemically determined hydroxylations and enzymhisto-chemically determined NADPH-nitro-BT reductase and Naphthol-AS-D esterase. No correlation was found between glucose-6-phosphate dehydrogenase or iso-citric acid dehydrogenase activity and hydroxylations. The difference in hydroxylating capacity between male and female rats may be caused by the fact that the number of cells with hydroxylating activity in the liver lobule, as judged by the NADPH-nitro-BT reductase and Naphthol-AS-D esterase activity, is higher in male than in female rats.
TL;DR: It was apparent that clostridial pectinesterase must hydrolyze methyl groups in highly esterified pectins with an action pattern similar to that of the lyase, which would be impossible for the two enzyme rates to have corresponded on the basis of a 2:1 ratio.
Abstract: Exopolygalacturonate lyase and pectinesterase from Clostridium multifermentans were assayed simultaneously in the same reaction mixture which contained a highly esterified pectin, polymethyl polygalacturonic acid methyl glycoside. Lyase is specific for unesterified galacturonide residues and cannot degrade this substrate in the absence of the esterase. The rate for esterase was twice the rate for lyase throughout the entire course of the combined reaction. Thus, the molar ratio of the two enzyme activities was the same since the product of the lyase is an unsaturated digalacturonic acid containing two free carboxyl groups. Since clostridial exopolygalacturonate lyase is known to degrade polygalacturonate in a linear manner beginning from the reducing ends of polygalacturonate chains, it was apparent that clostridial pectinesterase must hydrolyze methyl groups in highly esterified pectins with an action pattern similar to that of the lyase. Otherwise it would be impossible for the two enzyme rates to have corresponded on the basis of a 2:1 ratio.
TL;DR: These experiments showed that the genetic loci which control the enzymes of systems 1, 2 and 3 control isozymes that respond identically with the test reagents in their respective systems.
Abstract: Esterases found in rabbit erythrocytes and platelets were separated by zone electrophoresis in starch gels. Activity tests in various substrates were used to classify the esterase bands into four major categories. The bands of each category were further subdivided into groups by the effects of various inhibiting and activating agents. These experiments showed that the genetic loci which control the enzymes of systems 1, 2 and 3 control isozymes that respond identically with the test reagents in their respective systems. Diisopropyifluorophosphate and eserine sulfate inhibition indicated that the active sites of systems 1 and 2 enzymes are different. This supported the conclusion that the esterases of systems 1 and 2 are the products of closely linked loci and not multiple alleles at a single locus. Carbonic anhydrases which migrated in the cathodal portion of the gel were identified by their sensitivity to acetazolamide and more intense staining with $- rather than anaphthyl acetate as substrate. Carboxylic acid esters of naphthols, phenols and alcohols are hydrolyzed by esterases. In addition to their hydrolytic activity, some esterases are capable of catalyzing synthetic substrates. a- and �3-Naphthol substrates have been used as a method for distinguishing between the simple fatty acid esterases and true lipases (16).
TL;DR: Zymograms reveal a multiplicity of esterase isozymes in rabbit serum and most of the staining activity is concentrated in a region of the gels just anodal to the albumins where six phenotypes are distinguished.
Abstract: Zymograms reveal a multiplicity of esterase isozymes in rabbit serum. Most of the staining activity is concentrated in a region of the gels just anodal to the albumins where six phenotypes (A, AF, F, M, P, and S) are distinguished. The atropinesterase activity is associated with phenotypes A and AF and appears to be restricted to a single isozyme, zone A. Cocainesterase activity is limited to isozyme S, a zone common to all phenotypes except M.
TL;DR: The inability of the bacterial esterase to react with a synthetic peptide suggests that residual esterases activity associated with certain proteolytic enzymes is not involved, and heat denaturation and metal inhibition studies suggest that the ester enzyme activity is truly enzymic.
Abstract: SUMMARY: Fifty-two strains, comprising six Rhizobium species, were examined for their esterase patterns using electrophoresis on cellulose acetate. Esterase activity was detected in five Rhizobium species. The sixth species, R. japonicum, was characterized by the absence of esterase activity in all but one of the strains examined. Rhizobium trifolii and R. leguminosarum strains showed similarities in their esterase profiles. Rhizobium meliloti strains formed a group distinct from these on the basis of their esterase patterns. Rhizobium lotus sp. and R. phaseoli also exhibited esterase activity.
Heat denaturation and metal inhibition studies suggest that the esterase activity is truly enzymic. The inability of the bacterial esterase to react with a synthetic peptide suggests that residual esterase activity associated with certain proteolytic enzymes is not involved. Heat tests revealed differences in the sensitivity of the multiple forms of esterases in rhizobia to inactivation.
TL;DR: The pH versus proteinase activity curve (casein or hemoglobin plus urea substrate) for homogenates of unfertilized Lytechinus eggs reveals two regions of maximum activity: one between pH 3.5 and 4.3, and another of far greater magnitude from pH 8.0 to 11.0.
Abstract: The pH versus proteinase activity curve (casein or hemoglobin plus urea substrate) for homogenates of unfertilized Lytechinus eggs reveals two regions of maximum activity: one between pH 3.5 and 4.3, and another of far greater magnitude from pH 8.0 to 11.0. The two classes of proteinases can be separated on a sucrose density gradient. Both the acid and alkaline proteinases in homogenates prepared in isotonic monovalent salt solutions are remarkably stable at pH 7.4 and 0°C. Using synthetic peptide substrates, an enzyme with the specific esterase activity of chymotrypsin was demonstrated; this enzyme accounts for the major part of the proteinase activity at alkaline pH. In addition, an enzyme with specific esterase activity of trypsin was shown to be present, but of low activity. The proteinase activity at acid pH is largely due to an enzyme resembling cathepsin D. The data also suggest the presence of cathepsin B and cathepsin IV (or catheptic carboxypeptidase).
When eggs are homogenized in isotonic NaCl plus KCl at pH 7.4, 0.02 M tris buffer at 0°C, all of the alkaline proteinase, and 85–90% of the acid proteinase activity is sedimented at 10,000 g. The presence of any proteinase activity in the supernatant phase represents an artifact of the preparative procedures used. The granules which possess the proteinase activity are contained entirely in the yolk fractions; and the acid proteinase is contained in a population of granules which sediment more readily than those which contain the alkaline proteinase. The acid proteinase resembles the lysosomal acid hydrolases in that it is readily released from the particulates; in contrast, the alkaline proteinase is bound relatively firmly.
In contradistinction to reports in the literature, no changes in proteinase activity nor intracellular distribution could be detected following fertilization.