Showing papers in "Journal of Biological Chemistry in 1964"

TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.

TL;DR: The present paper gives a detailed account of the investigations on rabbit liver microsomes and crude microsomal digests, which have led to postulate the hemoprotein nature of the pigment.

TL;DR: This is a record of the concentrations of the nonenzyme components of the Embden-Meyerhof system in mouse brain measured at brief intervals after the production of complete ischemia by decapitation, which resulted in increases in glycolytic rates of at least 4to 7-fold in different experimental groups of mice.

TL;DR: It has now been possible to demonstrate that brain, adrenal medulla, and sympathetically innervated tissues contain a specific hydroxylase that catalyzes the conversion of L-tyrosine to dopa.

TL;DR: The CDP-reductase system was purified from E. coli 13 a low molecular weight, heat-stable protein, hereafter called thioredoxin, and the requirement for reduced lipoate was replaced by either catalytic amounts of thiOREDoxin + TPNH or substrate amounts of chemically reduced dihydrothiored toxin.

TL;DR: The results of electron spin resonance and optical spectrophotometry correlated with rapid reaction studies, to establish whether or not intermediate forms of the enzyme react at rates sufficient to account for its catalytic activity as discussed by the authors.

TL;DR: The combined analytical and kinetic information makes it seem likely that along the glycol.ytic pathway in mouse brain (a) no step is limited by the amount of enzyme present; (b) equilibrium is approximated at five or possibly six steps even during maximal glycolysis; (c) one step never reaches equilibrium; and (d) the hexokinase and phosphofructokinase steps are the only points at which there is absolute control of Glycolytic flux.

TL;DR: A lipase activity present in adipose tissue of both rats and rabbits which exhibits a marked specificity for hydrolysis of monoglycerides is investigated and evidence indicating that this activity is distinct from the hormone-sensitive lipase activit’y and probably also from lipoprotein lipase is presented.

TL;DR: This report concerns the purification, properties, distribution, and specificity of a neutral proteinase from the soluble fraction of rat brain.

TL;DR: The amino acid compositions of the various lactic dehydrogenases, with the exception of cysteine and tryptophan, were obtained according to the procedure of Moore, Spackman, and Stein (9).

TL;DR: Isolated mitochondria of various tissues have been found to accumulate large amounts of Ca++ and phosphate from the medium in a process stoichiometrically dependent on high energy intermediates generated by the energy-conserving mechanisms of the respiratory chain.

TL;DR: The specificity of the enzyme in attacking native double stranded DNA and its inability to act on small polynucleotides make it a unique and useful reagent in studies of DN-4 structure and metabolism.

TL;DR: It is revealed that exonuclease I attacks only at the 3'-hydroxyl end of a deoxyribo-oligonucleotide and that a free 3’-Hydroxyl group is essential for enzymatic activity.

TL;DR: Evidence is presented on the stoichiometry between active transport and adenosine tripbosphate hydrolysis and on the intracellular localization of the active site of the transportAdenosine triphosphatase activity.

TL;DR: These experiments demonstrated that only a portion of the fatty acids that are esterified with the /3 position of the dietary triglycerides undergo hydrolysis during the processes of digestion and absorption, and it is possible to elucidate the composition of the lipids that are absorbed, the way they arise by enzymatic Hydrolysis, and how they are subsequently resynthesized into the triglycerides that are found in the lymph.

TL;DR: Experiments dealing with the formation of long chain fatty acid esters of cholesterol with rat liver preparations found that the bulk of hydrolytic enzyme activity is present in the soluble fraction of the liver homogenate.

TL;DR: The ability of this DNA phosphatase activity to remove the 3’-phosphoryl end groups of high molecular weight oligonucleotides provides a useful reagent for studying the effect of such end groups in the DNA-synthesizing system.