The Distinction Between y-Glutamylhydroxamate Synthetase and L-Glutamine- Hydroxylamine Glutamyltransferase Actitviies in Rat Tissues STUDIES IN VIVO By ANNEMARIE HERZFELD and NATHAN

نویسنده

  • A. ESTES
چکیده

The formation of y-glutamylhydroxamate by homogenates under optimum assay condition showed an inconstancy in the ratios of the enzyme activities utilizing L-glutamate and ATP (y-glutamylhydroxamate synthetase) and L-glutamine and ADP (L-glutaminehydroxylamine glutamyltransferase) in a number of normal and neoplastic rat tissues. Although y-glutamylhydroxamate synthetase activities in adult livers and kidneys were identical in males and females, L-glutamine-hydroxylamine glutamyltransferase activities in the organs of females were significantly lower. The developmental formations of the two activities in liver, kidney, brain and muscle were not simultaneous. The L-glutamine-hydroxylamine glutamyltransferase activity in foetal liver or neonatal kidney could be prematurely evoked by thyroxine, but the y-glutamylhydroxamate synthetase activity remained unchanged. Injections of cortisol also had dissimilar effects on the two activities in thymus and hepatomas. The discrepant tissue distribution, asynchronous developmental formation and differential response to several hormonal stimuli provide evidence in vivo that the two activities are not catalysed by the same protein.

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

STUDIES IN VITRO By ANNEMARIE HERZFELD

Two common ways of measuring the potential for glutamine synthesis in a tissue are the rates of formation of y-glutamylhydroxamate either by synthesis from glutamate (the glutamylhydroxamate synthetase reaction) or by transfer from glutamine (the glutamyltransferase reaction); it has not been established, however, that either reaction is a specific measure of glutamine synthetase. By differenti...

متن کامل

A comparison of hydroxylamine and N-methylhydroxylamine as probes for the mechanism of action of the anthranilate synthetase of Escherichia coli.

In the presence of hydroxylamine, anthranilate synthetase catalyzes the formation of y-glutamylhydroxamate. This activity requires enzyme, glutamine, and hydroxylamine and is stimulated by chorismate and inhibited by tryptophan. Measurement of the absorption at 500 nm of the red-violet y-glutamylhydroxamate-Fea+ chelate provides a convenient assay for the glutaminase activity of this enzyme. Wh...

متن کامل

Assay for glutamine synthetase activity.

The use of phosphoenolpyruvate plus pyruvate kinase as an ATP-generating system in the assay for glutamine synthetase activity via the formation of gamma-glutamylhydroxamate from glutamate and hydroxylamine with crude tissue preparations is shown to give values far in excess of the true glutamine synthetase activity of the tissue. This is due to the generation of pyruvate, which reacts with hyd...

متن کامل

Glutamine synthetase in muscle and kidney.

1. Glutamine synthetase activity has been determined in extracts of rat cardiac and skeletal muscle and kidney, after treatment to ensure that the rate of synthesis was proportional to time of incubation and to amount of extract added. The activity was measured by two methods, with hydroxylamine as substrate. 2. No activity was detected in rat heart extract by either method. The activity in ske...

متن کامل

Studies of the mechanism of anthranilate synthase. Evidence for an acyl-enzyme.

The mechanism of anthranilate synthase reaction was studied using hydroxylamine as an inhibitor. Changes in the NH,OH concentration result in a concomitant alteration in the rates of synthesis of y-glutamylhydroxamate and anthranilate. However, the sum of the two products appears to be constant. Moreover, the degree of inhibition elicited by NHsOH at different concentrations is similar for the ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2005