نتایج جستجو برای: isoenzyme electrophoresis

تعداد نتایج: 54597  

Journal: :Plant physiology 2007
Matthew Peter Purnell José Ramon Botella

Glutamate (Glu) dehydrogenase (GDH, EC 1.4.1.2-1.4.1.4) catalyzes in vitro the reversible amination of 2-oxoglutarate to Glu. The in vivo direction(s) of the GDH reaction in higher plants and hence the role(s) of this enzyme is unclear, a situation confounded by the existence of isoenzymes comprised totally of either GDH beta- (isoenzyme 1) or alpha- (isoenzyme 7) subunits, as well as another f...

Journal: :Clinical chemistry 1984
D L Smalley B Womack C Handorf S Acchiardo

A 65-year-old woman failed to develop increased creatine kinase or lactate dehydrogenase activity after a myocardial infarction. She had no measurable creatine kinase MB isoenzyme and no detectable patterns of normal LD isoenzyme activity. These determinations five months after the infarction showed normal values for total activity and isoenzyme patterns.

Journal: :Clinical chemistry 1979
S A Cohen L Sideman

(b) by adding antiserum to the B sub-unit of CK to a portion of a patient's sample and the control, then electro-phoresing the untreated and treated aliquots in adjacent positions on the same agarose film. On inspecting the films before enzyme substrate was added, we would see fluorescent bands cathodal and anodal, adjacent to but distinct from the position where the BB isoenzyme would be expec...

Journal: :Clinical chemistry 1979
V Prabhakaran D A Nealon A R Henderson

In vitro incubation, at 37 degrees C, of human creatine kinase isoenzyme-1 (isoenzyme BB) and human immunoglobulin G in a buffer results in the formation of a complex of high relative molecular mass (Mr approximately 825,000), which contains both proteins. This complex also forms in vitro if creatine kinase isoenzyme-1 is incubated with fresh human serum. The creatine kinase activity of the com...

Journal: :Journal of clinical pathology 1982
S H Tsung

The effect of gastrointestinal surgery on serum creatine kinase activity was studied in 30 patients. The MB isoenzyme was demonstrated in sera of 30% of the patients and BB isoenzyme in 23%. MB content varied from 0.8 to 10.3% of the total creatine kinase activity, and the BB content from 0.6 to 18.4%. The CK-BB was probably of gastrointestinal origin, since gastrointestinal tract contains high...

Journal: :Clinical chemistry 1987
G C Moses A R Henderson

We describe a case of a limb-girdle myopathy presenting with myoglobinuria. A partial deficiency of muscle carnitine palmitoyltransferase (EC 2.3.1.21) may also have been present. All "muscle-type" serum enzymes were markedly increased (to between 30- and 400-fold their respective upper reference limits) and creatine kinase (EC 2.7.3.2) isoenzyme 2 (CK-MB) was increased 130-fold but was still l...

Journal: :Clinical chemistry 1978
H Aleyassine D B Tonks M Kaye

We assessed the reported presence of creatine kinase-BB isoenzyme in the serum of patients with chronic renal failure. Our study showed that the blood of these patients contains a fluorescent material with an electrophoretic mobility similar to that of the BB isoenzyme on cellulose acetate strips. The fluorescing material is, however, completely distinct from BB isoenzyme and its nature is as y...

Journal: :Clinical chemistry 1975
D W Mercer M A Varat

We describe a spectrophotometric kinetic assay for detecting creatine kinase MB isoenzyme activity in the 1 to 10 U/liter range. The MB isoenzyme was isolated [Clin. Chem. 20, 36 (1974)] and assayed (Rosalki method) with an Abbott ABA-100. Good reproducibility was demonstrated for MB isoenzyme activities near 1 U/liter (CV = 2.6%). Sera with normal or slightly increased total creatine kinase ac...

Journal: :Clinical chemistry 1982
T Komoda S Hokari M Sonoda Y Sakagishi T Tamura

With p-nitrophenyl phosphate as the substrate, there reportedly is no organ-specific inhibition of alkaline phosphatase (EC 3.1.3.1) activity by L-phenylalanine. However, we found that at pH 10.0, with p-nitrophenyl phosphate as the substrate, L-phenylalanine obviously inhibits the alkaline phosphatase isoenzyme from human placenta, whereas there is little if any inhibition of the isoenzyme fro...

2005
Hiroko KADOWAKI

The isoenzymic forms of branched-chain amino acid aminotransferase in mitochondria of rat tissues were compared with the better-known cytosolic forms in order to find any regular pattern of expression of these isoenzymes during development. Mitochondria of all tissues examined except brain contained only a type-I isoenzyme differing from the cytosolic type-I isoenzyme in heat stability and acti...

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