نتایج جستجو برای: liver enzyme

تعداد نتایج: 546103  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1981
M M Hosey F Marcus

We have tested rat liver fructose-bisphosphatase (D-fructose-1,6-bisphosphate 1-phosphohydrolase, EC 3.1.3.11) and three other gluconeogenic fructose-bisphosphatases as substrates for the catalytic subunit of cyclic AMP-dependent protein kinase. In contrast to the rat liver enzyme, homogeneous preparations of mouse liver, rabbit liver, and pig kidney fructose-bisphosphatase could not be phospho...

Journal: :Cancer research 1969
P Ove O E Brown J Laszlo

Sephadex G-200 column chromatography of hepatoma DNA polymerase yields two peaks of enzyme activity. Peak I contains enzyme having a marked preference for denatured DNA, and the levels of this enzyme increase in proportion to tumor growth rate. Peak II contains the enzyme fraction having a moderate preference for native DNA. Normal and regenerating rat liver have a predominance of Peak II, in c...

Journal: :The Biochemical journal 1995
S Fujiwara T Noguchi

It is generally accepted that all of the allantoin-degrading enzymes (allantoinase, allantoicase, ureidoglycollate lyase and urease), used in purine degradation, were lost during mammalian evolution. However, surprisingly, ureidoglycollate lyase has been found in a mammalian tissue. Ureidoglycollate lyase was purified to homogeneity and characterized from rat-liver mitochondria. The apparent Km...

Journal: :The Journal of biological chemistry 1951
G D NOVELLI F J SCHMETZ

During work on coenzyme A (CoA), a method for the liberation of pantothenic acid from the coenzyme was worked out (1). The method involves the use of a combination of two enzymes; namely, intestinal phosphatase and an enzyme extractable from acetone powder of bird liver (chicken (2), duck, or pigeon). This procedure proved the most efficient pretreatment to liberate bound vitamin under conditio...

Journal: :The Biochemical journal 1982
B Burchell

1. Reconstitution of purified bilirubin UDP-glucuronyltransferase from Wistar-rat liver into Gunn-rat liver microsomes provides a better environment than phosphatidylcholine liposomes, such that the final specific activity of the Wistar-rat liver enzyme was increased up to 85 units/mg of protein. 2. Gunn- and Wistar-rat liver microsomes were equally effective for reconstitution of the purified ...

Journal: :iranian journal of public health 0
m.saadat d.d. farhud

protein tyrosine phosphatases (ptpases) regulate tyrosine phosphorylation of target proteins involved in several aspects of cellular functions. enzyme activities of the ptpases in cytosolic and particulate fractions of rat ascites hepatoma cell lines were determined and compared with those of normal rat liver. our present data revealed that although there was no neoplatic-specific alteration of...

Journal: :iranian biomedical journal 0
علی اصغر مشتاقی ali asghar moshtaghie ایرج جوادی iraj javadi غلام رضا فقهی golamreza feghhi

the activity of aspartate aminotransferase (ast) in human serum has been widely determined as a diagnostic aid in liver disease. in this study, the effect of aluminium on ast isoenzymes in relation to aluminium intoxified patients has been investigated. using gel filtration chromatography technique with sephacryl s-300, mitochondrial aminotransferase (m-ast) and cytosolic aminotransferase (c-as...

Journal: :Revista espanola de enfermedades digestivas : organo oficial de la Sociedad Espanola de Patologia Digestiva 2004
A González-Quintela J Campos R Alende A López-Soto S Tomé E Otero J A Torre

OBJECTIVE To evaluate the prevalence, associated factors, and time-course changes of abnormal liver enzyme serum levels in adult patients with Salmonella enteritidis enterocolitis. METHODS The clinical records of 104 patients (age range 15-86 years, 46.2% males) admitted to hospital because of S. enteritidis enterocolitis were reviewed. The prevalence of abnormal liver enzyme levels was evalu...

Journal: :The Journal of biological chemistry 1990
D E Ash F A Emig S A Chowdhury Y Satoh V L Schramm

Phosphoenolpyruvate carboxykinase from chicken liver mitochondria and rat liver cytosol catalyzes the phosphorylation of alpha-substituted carboxylic acids such as glycolate, thioglycolate, and DL-beta-chlorolactate in reactions with absolute requirements for divalent cation activators. 31P NMR analysis of the reaction products indicates that phosphorylation occurs at the alpha-position to gene...

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