نتایج جستجو برای: sulfhydryl enzyme

تعداد نتایج: 251093  

Journal: :Hypertension 1994
M A Creager M A Roddy

Endothelium-dependent vasodilation is impaired in patients with essential hypertension. The objective of this study was to determine whether long-term treatment with angiotensin-converting enzyme inhibitors improves endothelium-dependent vasodilation in forearm resistance vessels of patients with hypertension. Furthermore, since tissue thiols may be relevant to nitric oxide-mediated vasodilatio...

Journal: :The Journal of biological chemistry 1960
T E CONOVER R L PRAIRIE E RACKER

1. The reaction of mitochondrial adenosine triphosphatase (coupling factor 1) with iodine resulted in rapid loss of ATPase activity, disappearance of sulfhydryl groups, binding of iodine to the protein, and partial dissociation of the molecule. The extent of the changes observed depended on the molar ratio of iodine to protein in the reaction mixture. At a molar ratio of 50, more than 99% of th...

2003
M. TAHARA

Threonine deaminase (Lthreonine hydrolyase (deaminating), EC 4.2.1.16) has been purified approximately 700-fold from extracts of Clostridium tetanomorphum. Both threonine and serine can serve as substrates, but threonine is deaminated 5 to 10 times more rapidly than serine. Pyridoxal phosphate, a reducing agent, and alkaline pH are required for the deamination of either amino acid. A plot of th...

Journal: :The Journal of biological chemistry 1969
Z Bohak

Chicken pepsinogen was extracted from the forestomach of chicken and purified by the consecutive application of acetone precipitation, chromatography on diethylaminoethyl cellulose, and gel filtration on Sephadex G-100. The purified pepsinogen was homogeneous on disc electrophoresis and sedimented as monodisperse material. Chicken pepsin was obtained by the activation of the pure zymogen at pH ...

2018
Kazuo NAKAMuRA Hiroshi YosHiKAwA Sanae OKuBo Hiroshi KuRosAwA

with n-heptyl-fi-D-thioglucoside, and then purified by DEAE-Sepharose and hydroxylapatite columns containing Triton X-100. The puTified enzyme was electrophoretically homogeneous. The enzyme had an apparent molecular mass of 400kDa, and was composed of three subunits whose molecular masses were 74, 70, and 62 kDa. The purified enzyme was much more labile than the membrane-bound enzyme (membrane...

Journal: :Journal of bacteriology 1979
Y Ando

The exudate of fully germinated spores of Clostridium perfringens was found to contain a large amount of a spore lytic enzyme which acted directly on alkali-treated spores of the organism to cause germination. Although no detectable amount of the enzyme was found in dormant spores during germination in a KCl medium, the enzyme was produced rapidly and released into the medium. The optimal condi...

Journal: :The Journal of biological chemistry 1991
W Landgraf S Regulla H E Meyer F Hofmann

The functional significance of the oxidation/reduction state of sulfhydryl groups of cGMP-dependent protein kinase (cGMP kinase) was studied at 30 degrees C using different metal ions as oxidizing agents. Mn2+, Zn2+, Fe2+, Ni2+, and Co2+ failed to activate cGMP kinase, whereas Cu2+, Cu+, Fe3+, Hg2+, and Ag+ activated cGMP kinase by oxidation with an activity ratio (-cGMP/+cGMP) of about 0.7. Th...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2014
Cheryl A Kreinbring Stephen P Remillard Paul Hubbard Heather R Brodkin Finian J Leeper Dan Hawksley Elaine Y Lai Chandler Fulton Gregory A Petsko Dagmar Ringe

Thiaminases, enzymes that cleave vitamin B1, are sporadically distributed among prokaryotes and eukaryotes. Thiaminase I enzymes catalyze the elimination of the thiazole ring moiety from thiamin through substitution of the methylene group with a nitrogenous base or sulfhydryl compound. In eukaryotic organisms, these enzymes are reported to have much higher molecular weights than their bacterial...

Journal: :The Journal of biological chemistry 1962
E HABER C B ANFINSEN

Fully reduced ribonuclease (RNase), devoid of demonstrable secondary or tertiary structure, may be oxidized by molecular oxygen to yield a product which is indistinguishable by physical measurements or enzymatic activity from the native enzyme (2-4). Since reduced RNase contains eight sulfhydryl groups, 105 possible arrangements with four disulfide bridges may occur (5, 6), yet the native enzym...

Journal: :Zeitschrift fur Naturforschung. C, Journal of biosciences 1990
H Durchschlag P Zipper

The sulfhydryl enzyme malate synthase was inactivated by X-irradiation in air-saturated aqueous solution, in the absence or presence of a variety of additives (thiols, antioxienzymes, typical radical scavengers, inorganic salts, buffer components, substrates, products, analogues). Radiation-induced changes of enzymic activity were registered immediately after stop of irradiation and in the post...

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