Showing papers in "Analytical Biochemistry in 1971"

TL;DR: The staining procedure for localizing superoxide dismutase on polyacrylamide electrophoretograms has been applied to extracts obtained from a variety of sources and could thus be assayed either in crude extracts or in purified protein fractions.

TL;DR: Because of the importance of intrinsic charge and conformation, the system, although allowing a first approximation in molecular weight determination, may also be applicable to peptide “mapping,” particularly for “insoluble” peptide mixtures with prominent hydrophobic association, such as encountered in cellular membranes, viruses, and proteolytic digests.

TL;DR: A modification of the fluorometric assay of Kissane and Robins that uses a standard cell type instead of a standard DNA solution makes the assay universally reproducible.

TL;DR: The large molar absorptivity of 28,000 for the iron-ferrozine complex makes the ligand an attractive color reagent for monitoring iron therapy in anemic patients.

TL;DR: Relative mobility values for macromolecules in polyacrylamide gel electrophoresis at various gel concentrations are used to compute the retardation coefficient, KR, molecular radius, R, free mobility, M0, and valence, V.

TL;DR: Brain, NE, DA, and 5-HT can be assayed simultaneously from discrete samples by this method, which is based upon the alumina method described by Anton and Sayre, utilizing acid extraction of tissues and a single solvent step.

TL;DR: A rapid and simple method for determination of small amounts of sulfate present in glycosaminoglycans is described, which uses sodium rhodizonate, which in the presence of barium forms a red compound.

TL;DR: Collagen α-chains and collagen peptides exhibit a lower electrophoretic mobility in SDS-polyacrylamide electrophoresis than globular proteins of the same size and within these limits this method may be well suited for molecular weight estimations.

TL;DR: The current studies provided a better insight into the chemical basis for the chemical based for the delipidation of VLDL and HDL and also allowed for the design of procedures insuring total recoveries of delipidated apo V LDL and apo HDL (apo HDL2 and APO HDL3).

TL;DR: The specificity of the assay has been demonstrated in experiments in which various factors that influence either tyrosine hydroxylase or aromatic l-amino acid decarboxylase activity were omitted, and the sensitivity of the method has been shown to be greater in the laboratory than tyrosin hydroxyase assays currently used.

TL;DR: A simple and precise spectrophotometric determination of methanol in the range 2–40 μg is described, which is an improvement on previously described methods and the value of the method in studies of pECTin and pectin esterase metabolism is indicated.

TL;DR: A method is described for separating 3′,5′-nucleoside monophosphates from other nucleotides on columns of aluminum oxide and an α-32P-labeled nucleoside triphosphate provides a specific precursor for use in assaying cyclase enzymes.

TL;DR: A rapid, simple, one-step procedure is described for the separation of cyclic AMP from ATP, ADP, AMP, and P 1 based on selective adsorption of all nucleotides except cyclicAMP on hydrous aluminum oxide.

TL;DR: Gas-liquid chromatography allowed separation of the diastereoisomeric derivatives and thus provided a sensitive means for determination of the absolute configuration of the parent unsaturated hydroxy ester.

TL;DR: The collection of fractions from gradients is simplified by the substitution of a paper strip marked off into sections for the usual paper disc technique.

TL;DR: The thiosemicarbazide-diacetyl-monoxime-urea (TDMU) assay obviates these additional steps and has the advantage of being a direct colorimetric procedure applicable to crude enzyme preparations.

TL;DR: A small reversed-phase chromatographic system for the separation of [ 3 H] or [ 14 C] aminoacyl-tRNA's is described and has the advantages of speed, sensitivity, and excellent resolution of isoaccepting tRNA's.

TL;DR: A modern, miniaturized, solid-state photometer that possesses the stability and accuracy of the original Mac-Nichol design along with its calibrated gain settings is described.

TL;DR: Reaction of proteins with dansyl chloride in mildly alkaline SDS systems at high mole ratios of dANSyl chloride to protein yields dansyated proteins that can be run in SDS gel electrophoresis systems with no significant change in protein mobility.

TL;DR: A 3.7% T polyacrylamide gel allowed for isoelectric focusing of hemoglobin and cyanogen bromide fragments of both collagen and hemoglobin in the absence of significant molecular sieving and provided satisfactory mechanical stability.

TL;DR: The average pore diameter of the gels was sufficient to allow penetration of all but the very largest proteoglycans of articular cartilage, making it possible to distinguish “aggregates” from disaggregated molecules.

TL;DR: An improved direct spectrophotometric method is described that is suited to determinations of sulfide in enzyme mixtures and in biological materials and achieves major improvement in the method by quantitative precipitation of zinc sulfide and removal of the soluble components of the sample.

TL;DR: A rapid and simple method for estimation of the sulfate content of less than 1 μg of acidic glycosaminoglycans is presented.

TL;DR: In this paper, an analysis of the behavior of charged macromolecules in both linear and nonlinear gel gradients is presented, based on Ferguson's relationship for electrophoretic mobility versus gel concentration with the equation describing the gel gradient.

TL;DR: A gas chromatographic method for determining the neutral and amino sugars commonly found in glycoproteins of animal origin, which can be determined on as little as 1 mg of a glycoprotein which contains 6% total carbohydrate.

TL;DR: The detection of pyruvate kinase (PyK) activity after electrophoresis on cellulose polyacetate strips is presented, which is sensitive and selective and has the advantage of producing a permanent photographic record.

TL;DR: The catalytic activity of lysozyme measured in terms of chemical equivalents of substrate converted per unit time is quite low and an approximate relation has been determined between the amount of chemical reaction and an activity unit defined in terms the rate of absorbance change.