Showing papers on "Peptide sequence published in 1978"
2,751 citations
TL;DR: The number of differences in amino acid positions between IGF-I and insulins suggests that duplication of the gene of the common ancestor of proinsulin and IGF occurred before the time of appearance of the vertebrates.
1,531 citations
776 citations
TL;DR: The nucleotide sequence of the ampicillin resistance gene of pBR322, an Escherichia coli plasmid that encodes a penicillin beta-lactamase, is determined and the first 23 amino acids presumably form a signal for secretion.
Abstract: I have determined the nucleotide sequence of the ampicillin resistance gene of pBR322, an Escherichia coli plasmid that encodes a penicillin beta-lactamase. This gene codes for a protein of 286 amino acid residues. The first 23 amino acids presumably form a signal for secretion, because they do not appear in the mature enzyme, whose partial amino acid sequence has been determined independently.
772 citations
TL;DR: The protein chemical characterization of the amino-terminal tryptic peptide of actin from different bovine tissues shows that at least six different actin structural genes are expressed in this mammal.
706 citations
TL;DR: The complete nucleotide sequence of the DNA of bacteriophage φX174 has been determined and the amino acid sequences of the ten proteins for which the DNA codes have also been deduced.
608 citations
TL;DR: The structure of adenovirus 2 (Ad2) cytoplasmic RNAs produced during the early phase of infection is defined and it is suggested that, like the SV40 tumor antigens, the polypeptides encoded by these Ad2 mRNAs have an identical amino acid sequence at their N terminal ends, but have different C terminal sequences.
512 citations
TL;DR: The amino acid sequence of glycophorin AMN has been determined by manual Edman degradation, using both the direct Edman and the dansyl-Edman procedures simultaneously for determination of glycosylated amino acid residues.
Abstract: Peptides of glycophorin AMN were prepared by cyanogen bromide cleavage and by chymotryptic and tryptic digestion. Cyanogen bromide cleavage produces three fragments which account for the entire polypeptide chain. Trypsin and chymotrypsin cleave completely at several sites, but incompletely at sites within the glycosylated segment of the polypeptide chain. Some of the latter sites become accessible to proteolysis after desialation in addition to exposure of new sites for cleavage. The amino acid sequence of glycophorin AMN has been determined by manual Edman degradation, using both the direct Edman and the dansyl-Edman procedures simultaneously for determination of glycosylated amino acid residues. The automated procedure was used for sequence determination of a hydrophobic peptide. Glycophorin A is a polypeptide chain of 131 amino acid residues and contains 16 oligosaccharide units attached to the amino-terminal third of the molecule. Fifteen oligosaccharides are linked O-glycosidically to either threonine or serine residues and one complex oligosaccharide unit is attached N-glycosidically to an asparagine residue. Amino-terminal sequences are different for glycophorin AM and AN, the two forms of the glycophorin A molecule coded for by genes at the MN locus. The differences in sensitivity to proteases of various sites on glycophorin A seem to be due to heterogeneity in the carbohydrate components and not to differences in the primary structure of the polypeptide chains. This work contains a number of revisions and corrections of earlier preliminary reports [Segrest, J.P., Jackson, R. chem. Biophys. Res. Commun, 49, 964-969; Tomita, M., & Marchesi, V.T. (1975) Proc. Natl. Acad. Sci. U.S.A. 72, 2964-2968].
383 citations
TL;DR: The sequence of troponin I from fast and slow skeletal and cardiac muscle shows strong homology in the region which binds to actin and is responsible for inhibition of the actomyosin ATPase.
Abstract: The sequence of troponin I from fast and slow skeletal and cardiac muscle shows strong homology in the region which binds to actin and is responsible for inhibition of the actomyosin ATPase. More differences are found in the N-terminal region which binds to troponin C.
380 citations
TL;DR: The complete sequence of chicken ovalbumin mRNA is presented and an extensive 3′ noncoding region of 637 nucleotides which may have no function that is precisely dependent on its sequence is presented.
Abstract: The complete sequence of chicken ovalbumin mRNA is presented; it is 1,859 residues long, excluding its terminal 'cap' and poly(A). The region coding for ovalbumin lies close to the 'cap' but is separated from the poly(A) by an extensive 3' noncoding region of 637 nucleotides which may have no function that is precisely dependent on its sequence.
378 citations
TL;DR: The sequence confirms that the variable region gene lies on the DNA separated from the constant region of a mouse immunoglobulin light chain, the VlambdaII gene, andHypervariable region codons appear in the germ-line sequence.
Abstract: We have determined the sequence of the DNA of a germ-line gene for the variable region of a mouse immunoglobulin light chain, the VlambdaII gene. The sequence confirms that the variable region gene lies on the DNA separated from the constant region. Hypervariable region codons appear in the germ-line sequence. A sequence for the hydrophobic leader, 19 amino acids that are cleaved from the amino terminus of the protein, appears near, but not continuous with, the light chain structural sequence: most of the leader sequence is separated from the rest of the gene by 93 bases of untranslated DNA.
TL;DR: A detailed correlation of the amino acid sequence, conformation, and self association of A-I will add further insight into the molecular mechanisms involved in protein-protein and protein-lipid interactions.
TL;DR: A simple, non-empirical hypothesis is presented to account for both the turns and the hydrophobic core of the protein using only the amino acid sequence.
Abstract: Peptide chain turns are those parts of a globular protein where the backbone changes its direction. A simple, non-empirical hypothesis is presented to account for both the turns and the hydrophobic core of the protein using only the amino acid sequence.
TL;DR: The amino acid sequence of a brain-specific protein, S-100, has been determined by the analysis of four cyanogen bromide peptides and fourteen tryptic peptides derived from the protein.
Abstract: The amino acid sequence of a brain-specific protein, S-100, has been determined by the analysis of four cyanogen bromide peptides and fourteen tryptic peptides derived from the protein. The protein chain consists of 91 amino acid residues and has a molecular weight of 10 507. The sequence shows regions of strong clustering of hydrophobic, basic and acidic amino acids, with an apparent calcium-binding site in the acidic cluster.
TL;DR: Since these cleavages confer infectivity upon both Sendai and influenza viruses and the ability to induce cell-to-cell fusion upon Sendai virus, the hydrophobic NH2-terminal sequences on F1 and HA2 may play a role in fusion of viral and host-cell membranes.
Abstract: The two glycoproteins of Sendai virus, the hemagglutinin-neuraminidase and the fusion protein (F), were separated and purified by affinity chromatography on a Lens culinaris lectin-Sepharose column. F was shown to consist of two disulfide-bonded glycopolypeptide chains, F1 and F2, of molecular weights 51,000 and 11,000, each of which contained 15% carbohydrate by weight. Amino-terminal sequence analysis showed that F2 was blocked and that the hydrophobic sequence NH2-Phe-Phe-Gly-Ala-Val-Ile-Gly-Ile-Ile-Ala-Leu-Gly-Pro-Ala-Thr- was at the amino terminus of F1. This sequence shows identity at six positions with the hydrophobic amino-terminal sequence of the smaller glycopolypeptide chain, HA2, of the hemagglutinin of influenza virus. Both F1 and HA2 are formed by proteolytic cleavage of precursor glycoproteins (Fo, Sendai virus; HAo, influenza virus). Since these cleavages confer infectivity upon both Sendai and influenza viruses and the ability to induce cell-to-cell fusion upon Sendai virus, the hydrophobic NH2-terminal sequences on F1 and HA2 may play a role in fusion of viral and host-cell membranes.
TL;DR: A series of small peptides corresponding to the amino termini of the fibrin alpha-and beta-chains has been synthesized as discussed by the authors, and they have been shown to be potent inhibitors of fibrins polymerization.
Abstract: A series of small peptides corresponding to the amino termini of the fibrin alpha- and beta-chains has been synthesized. The peptides glycyl-L-prolyl-L-arginyl-L-proline and glycyl-L-prolyl-L-arginylsarcosine are potent inhibitors of fibrin polymerization. Moreover, these peptides have a natural stability stemming from their inherent resistance to proteolysis because of the involvement of amino acids in each of their peptide bonds. The peptide glycyl-L-prolyl-L-arginyl-L-proline binds to fibrinogen and to fragment D, in both cases with an association constant of approximately 5 x 10(4); it does not bind to fragment E. The number of binding sites is two for fibrinogen and one for fragment D. The tripeptide glycyl-L-prolyl-L-arginine binds less tightly and is less than half as effective in preventing polymerization. The peptide glycyl-L-histidyl-L-arginyl-L-proline, which corresponds exactly to the amino terminus of the fibrin beta-chain, does not inhibit the aggregation of fibrin monomers under the conditions used. It does bind weakly to fibrinogen, however, suggesting the involvement of sites other than those binding the alpha-chain analogues. Various other peptides were found not to inhibit polymerization; these included glycine-L-proline, L-prolyl-L-arginine and glycyl-L-prolyl-L-seryl-L-proline. The last-named corresponds to the serine/arginine amino acid replacement previously reported for a defective human fibrinogen.
TL;DR: The sequence of 35 residues at the NH2 terminus of ovalbumin was determined by automated Edman degradation after a method was devised to prevent acetylation during protein synthesis in the reticulocyte lysate, and does not resemble the transient "signal peptides" associated with most secretory proteins.
Abstract: Ovalbumin mRNA was translated in a reticulocyte lysate. The primary translation product starts with methionine derived from Met-tRNAf. When the nascent polypeptide is about 20 residues long, this methionine is removed. The new NH2-terminal glycine is acetylated from acetyl-CoA when the polypeptide is 44 residues long. The sequence of 35 residues at the NH2 terminus of ovalbumin was determined by automated Edman degradation after a method was devised to prevent acetylation during protein synthesis in the reticulocyte lysate. This sequence is the same as that of secreted ovalbumin and does not resemble the transient "signal peptides" associated with most secretory proteins, including three other egg white proteins synthesized in the same cells as ovalbumin.
TL;DR: Muscle and cytoplasmic actins from several species have been compared by extensive fingerprint analysis and by partial amino acids sequence determination with the known amino acid sequence of rabbit muscle actin and the following characteristics are apparent.
Abstract: Muscle and cytoplasmic actins from several species have been compared by extensive fingerprint analysis and by partial amino acid sequence determination with the known amino acid sequence of rabbit muscle actin. Although complete sequences have not been established, the following characteristics are apparent. (a) Cytoplasmic actins are the products of two different genes. The difference seen in isoelectric focusing studies is probably determined only by the nature of the three amino-terminal acidic residues. (b) Mammalian cytoplasmic actins are exceedingly similar and perhaps identical. (c) Cytoplasmic actins may differ by at least 25 amino acid replacement from rabbit muscle actin. These replacements have been identified for calf thymus actin; however, other cytoplasmic actins show the same replacements. (d) The replacements always involve—except for the first five residues—neutral amino acid residues. (e) The replacements are not randomly distributed. Residues 18-75 are constant whereas residues 2-18 and 259-298 show many substitutions. (f) The main component of smooth muscle actin from chicken gizzard shows the charge characteristics found at the amino terminus of the less acidic cytoplasmic actin species. In the rest of the polypeptide chain, gizzard actin resembles skeletal muscle actin, although two substitutions of the cytoplasmic type have been identified. (g) Heart muscle actin is very similar to skeletal muscle actin. Only two amino acid replacements have been found; they are of the cytoplasmic type. (h) Skeletal muscle actins from chicken and beef have not shown a replacement.
TL;DR: Differences in amino acid sequence of erythrocyte membrane glycophorin A are correlated with M or N blood group activity, suggesting that different structural genes code for the glycoproteins carrying these antigens.
Abstract: Differences in amino acid sequence of erythrocyte membrane glycophorin A are correlated with M or N blood group activity. A second sialoglycoprotein, glycophorin B, has an amino acid sequence identical to that of glycophorin AN in the first 23 positions and carries N activity only, suggesting that different structural genes code for the glycoproteins carrying these antigens. Certain genetically variant cells lack glycophorin A, as determined by immunochemical methods, and serological MN activity. Other variants lack MN activity, but contain normal amounts of glycophorin A in the membrane.
TL;DR: The mechanism of activation of human Factor IX and its inhibition by antithrombin III is essentially identical to that previously shown for bovine Factor IX.
Abstract: Human Factor IX (Christmas factor) is a single-chain plasma glycoprotein (mol wt 57,000) that participates in the middle phase of the intrinsic pathway of blood coagulation. It is present in plasma as a zymogen and is converted to a serine protease, Factor IXabeta, by Factor XIa (activated plasma thromboplastin antecedent) in the presence of calcium ions. In the activation reaction, two internal peptide bonds are hydrolyzed in Factor IX. These cleavages occur at a specific arginyl-alanine peptide bond and a specific arginyl-valine peptide bond. This results in the release of an activation peptide (mol wt approximately equal to 11,000) from the internal region of the precursor molecule and the generation of Factor IXabeta (mol wt approximately equal to 46,000). Factor IXabeta is composed of a light chain (mol wt approximately equal to 18,000) and a heavy chain (mol wt approximately equal to 28,000), and these chains are held together by a disulfide bond(s). The light chain originates from the amino terminal portion of the precursor molecule and has an amino terminal sequence of Tyr-Asn-Ser-Gly-Lys. The heavy chain originates from the carboxyl terminal region of the precursor molecule and contains an amino terminal sequence of Val-Val-Gly-Gly-Glu. The heavy chain of Factor IXabeta also contains the active site sequence of Phe-Cys-Ala-Gly-Phe-His-Glu-Gly-Arg-Asp-Ser-Cys-Gln-Gly-Asp-SER-Gly-Gly-Pro. The active site serine residue is shown in capital letters. Factor IX is also converted to Factor IXaalpha by a protease from Russell's viper venom. This activation reaction, however, occurs in a single step and involves only the cleavage of the internal arginyl-valine peptide bond. Human Factor IXabeta was inhibited by human antithrombin III by the formation of a one-to-one complex of enzyme and inhibitor. In this reaction, the inhibitor was tightly bound to the heavy chain of the enzyme. These data indicate that the mechanism of activation of human Factor IX and its inhibition by antithrombin III is essentially identical to that previously shown for bovine Factor IX.
TL;DR: The C5a molecule is one of two spasmogenic fragments released from serum components C3 and C5 during complement activation and its structural features are compared with those of the chemotactically active formyl-Met peptides to indicate their common genetic ancestry.
TL;DR: The complete primary structure of the platelet-specific protein human beta-thromboglobulin has been determined and shows a marked homology with that of platelet factor 4.
Abstract: The complete primary structure of the platelet-specific protein human beta-thromboglobulin has been determined. beta-Thromboglobulin consists of identical subunits of 81 amino acids, each with a molecular weight of 8851. The amino acid sequence of the beta-thromboglobulin subunit is: Gly-Lys-Glu-Glu-Ser-Leu-Asp-Ser-Asp-Leu-Tyr-Ala-Glu-Leu-Arg-Cys-Met-Cys-Ile-Lys-Thr-Thr-Ser-Gly-Ile-His-Pro-Lys-Asn-Ile-Gln-Ser-Leu-Glu-Val-Ile-Gly-Lys-Gly-Thr-His-Cys-Asn-Gln-Val-Glu-Val-Ile-Ala-Thr-Leu-Lys-Asp-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Pro-Asp-Ala-Pro-Arg-Ile-Lys-Lys-Ile-Val-Gln-Lys-Lys-Leu-Ala-Gly-Asp-Glu-Ser-Ala-Asp. Disulfide bridge-18 to half-cystine-58. The amino acid sequence of beta-thromboglobulin shows a marked homology with that of platelet factor 4. When the sequences are aligned for maximum homology, 42 of the 81 residues of beta-thromboglobulin are identical with those of platelet factor 4, including the position of the four half-cystines.
TL;DR: The results obtained show that all three mammalian cytoplasmic actins studied contain the same amino-acid exchanges indicating that mammalian cy toplasmi actins are very similar if not identical in amino- acid sequence.
Abstract: Actin was purified from calf thymus, bovine brain and SV40-transformed mouse 3T3 cells grown in tissue culture. Isoelectric focusing analysis showed the presence of the two actin polypeptides beta and gamma typical for non-muscle actins in all three actins. Tryptic and thermolytic peptides accounting for the complete amino-acid sequence of the cytoplasmic actins were separated and isolated by preparative fingerprint techniques. All peptides were characterized by amino-acid analysis and compared with the corresponding peptides from rabbit skeletal muscle actin. Peptides which differed in amino-acid composition from the corresponding skeletal muscle actin peptides were subjected to sequence analysis in order to localize the amino-acid replacement. The results obtained show that all three mammalian cytoplasmic actins studied contain the same amino-acid exchanges indicating that mammalian cytoplasmic actins are very similar if not identical in amino-acid sequence. The presence of two different isoelectric species beta and gamma in cytoplasmic actins from higher vertebrates is acccounted for by the isolation of two very similar but not identical amino-terminal peptides in all three actin preparations. The nature of the amino-acid replacements in these two peptides not only accounts for the different isoelectric forms but also shows that beta and gamma cytoplasmic actins are the products of two different structural genes expressed in the same cell. The total number of amino-acid replacements so far detected in the comparison of these cytoplasmic actins and skeletal muscle actin is 25 for the beta chain and 24 for the gamma chain. With the exception of the amino-terminal three or four residues, which are responsible for the isoelectric differences, the replacements do not involve charged amino acids. The exchanges are not randomly distributed. No replacements were detected in regions 18--75 and 299--356 while the regions between residues 2--17 and 259--298 show a high number of replacements. In addition documentation for a few minor revisions of the amino acid sequence of rabbit skeletal muscle actin is provided.
TL;DR: The amino acid sequence of the large cyanogen bromide fragment derived from the NH2-terminal half of alpha-tropomyosin has been determined and analysis of the sequence has permitted rational explanations for the stabilization of its coiled-coil structure.
TL;DR: The isolation (using calcium-dependent affinity chromatography) of proteins closely resembling human SAP, from sera of other mammals, amphibia and fish, and of proteins from the plaice and the chicken are reported for the first time.
Abstract: TWO apparently disparate human plasma proteins, C-reactive protein (CRP) and amyloid P component (protein SAP)1, have been shown to have substantial homology of amino acid sequence, similar subunit composition and similar molecular appearance in the electron microscope2. We now report for the first time the isolation (using calcium-dependent affinity chromatography) of proteins closely resembling human SAP, from sera of other mammals, amphibia and fish, and of proteins from the plaice (Pleuronectes platessa L.) and the chicken, which closely resemble human CRP. The stable evolutionary conservation in this plasma protein family of calcium-dependent ligand-binding specificity and molecular architecture during much of vertebrate evolution implies that they have important functions, and also facilitates their experimental investigation.
TL;DR: The amino-terminal amino acid sequences of the pili proteins from four antigenically dissimilar strains of NeISSeria gonorrhoeae, from Neisseria meningiditis, and from Escherichia coli were determined and imply a role for the amino- terminus structure in pilus function.
Abstract: The amino-terminal amino acid sequences of the pili proteins from four antigenically dissimilar strains of Neisseria gonorrhoeae, from Neisseria meningiditis, and from Escherichia coli were determined. Although antibodies raised to the pili protein from a given strain of gonococcus cross-reacted poorly or not at all with each of the other strains tested, the amino-terminal sequences were all identical. The meningococcal protein sequence was also identical with the gonococcal sequence through 29 residues, and this sequence was highly homologous to the sequence of the pili protein of Moraxella nonliquifaciens determined by other workers. However, the sequence of the pili protein from E. coli showed no similarity to the other sequences. The gonococcal and meningococcal proteins have an unusual amino acid at the amino termini, N-methylphenylalanine. In addition, the first 24 residues of these proteins have only two hydrophilic residues (at positions 2 and 5) with the rest being predominantly aliphatic hydrophobic amino acids. The preservation of this highly unusual sequence among five antigenically dissimilar Neisseria pili proteins implies a role for the amino-terminal structure in pilus function. The amino terminus may be directly or indirectly (through preservation of tertiary structure) important for the pilus function of facilitating attachment of bacteria to human cells.
TL;DR: An inverted membrane vesicle fraction isolated from uninfected Escherichia coli and largely derived from the inner membrane has been shown to contain an endoproteolytic activity that cleaves nascent bacteriophage f1 pre-coat protein into two identifiable products.
Abstract: An inverted membrane vesicle fraction isolated from uninfected Escherichia coli and largely derived from the inner membrane has been shown to contain an endoproteolytic activity that cleaves nascent bacteriophage f1 pre-coat protein into two identifiable products. The electrophoretic mobility on sodium dodecyl sulfate/urea/polyacrylamide gels and the partial amino-terminal sequence of the larger fragment were indistinguishable from those of the mature phage coat protein. Partial amino-terminal sequence analysis showed that the smaller fragment corresponds to the amino-terminal "signal peptide" of f1 pre-coat protein. Cleavage occurred only if the membrane fraction was present during in vitro synthesis, and was not observed if it was added after completion of pre-coat protein synthesis. The cleavage reaction was strongly stimulated when the membrane fraction was present together with the nonionic detergent Nikkol. These results are consistent with and discussed in terms of the signal hyothesis.
TL;DR: The ability of various peptides derived by proteolytic digestion of alpha1(I)-CB7 to bind to c-CAP based upon their ability to inhibit cell attachment to collagen is examined.
TL;DR: The three-dimensional structure of bovine liver rhodanese, a mitochondrial sulfurtransferase, has been determined at 2.5 A resolution using the multiple isomorphous replacement technique as mentioned in this paper.
TL;DR: The amino acid sequence of beta-galactosidase has been determined and all 80 tryptic peptides as well as all 24 CNBr peptides have been isolated in pure form.