Showing papers in "Journal of Biological Chemistry in 1956"

TL;DR: Compounds Used-N”l-Acetyl-n-ornithine was synthesized as previously described and L-Ornithine monohydrochloride was obtained from the Mann Research Laboratories.

TL;DR: The present investigation was undertaken to determine quantitatively the stability of each of the amino acid residues in the ribonuclease molecule under the conditions employed for the oxidation of the cystine sulfur bridges.

TL;DR: The ratio of P32 to Cl4 in the product was closely similar to that of the labeled P-choline, suggesting incorporation of both phosphorus and choline as an intact unit into a phospholipide, presumably lecithin.

TL;DR: A sensitive calorimetric method for the quantitative determination of SAL is described and 6AL has been found in urine of a patient with acute porphyria and also in normal urine.

TL;DR: This method is a modification of procedures for the determination of dextran and biood sugar, with critical studies of procedures based upon extraction of tissues with 30 per cent KOH and with 5 per cent TCA.

TL;DR: In the present study, the chemical structure of ribonuclease has been investigated by the use of trypsin as a reagent for the hydrolysis of specific peptide bonds in the oxidized protein, and the resulting peptides have been separated and analyzed by ion exchange chromatography.

TL;DR: Rabbit liver mitochondria used only for the experiments in Table I were prepared by grinding the tissue in 0.25 M sucrose in a Waring blendor at reduced speed and suspended in 1 ml.

TL;DR: An enzyme is found in chicken liver that catalyzes the net synthesis of triglyceride according to the following equation:.

TL;DR: The procedures described here have resulted in greater yields of enzyme with a higher specific activity than reported previously, even though apparently homogeneous preparations of liver phosphorylase were obtained by an earlier procedure.

TL;DR: Results suggested that the amino acids were being activated as an amino acyl AMP compound, given further support by the finding that a-amino hydroxamic acids are formed in the presence of high hydroxylamine concentrations, with concomitant loss of ATP.

TL;DR: Work from this Laboratory indicated that the presence of uracil inhibited formation of pyridine intermediates earlier than erotic acid in pyrimidinerequiring E. coli mutants, and it seemed of interest to determine whether this observation plus the above facts could be the results of normal selfregulatory mechanisms of the cell which allowed formation of no more.

TL;DR: It has been found that guanosine dior triphosphate is required in addition to ATP for amino acid incorporation in an enzyme system from rat liver which catalyzes the incorporation of labeled amino acids into proteins under anaerobic conditions.

TL;DR: The work presented here was completed and two reports appeared on the influence of phenylmercuric acetate and dinitrophenol on myosin ATPase, which appear to be dealing with similar phenomena.

TL;DR: This paper deals with the liberation of the cytochrome from its particulate complex, the fractionation steps in its purification, electrophoretic and ultracentrifugal tests for homogeneity, molecular weight determination, spectral properties, and reactions with a number of reagents.

TL;DR: In a medium containing the twelve amino acids previously shown to be essential, the seven demonstrably essential vitamins, glucose, electrolytes, and serum protein, both the mouse fibroblast and the human carcinoma cell degenerated and died unless the medium was supplemented with glutamine.

TL;DR: The present communication is concerned with an enzyme from spinach which catalyzes the formation of PGA from RuDP and CO2 as shown in equation (1) .2 This reaction does not appear to be reversible at neutral.

TL;DR: The specificity of lipase for the primary hydroxyl groups of glycerides is indicated by the recent report of Borgstrom (7), and it will be impossible to demonstrate any specificity which the enzyme may have for particular long chain fatty acids.

TL;DR: Analysis of the enzymatic activity of pyridine-substituted DPN analogues shows that not only does APDPN react with dehydrogenases, but in some cases actually reacts faster than DPN.