The inhibition of horse-liver esterase by rhodamine B
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چکیده
منابع مشابه
Inhibition of Horse Liver Alcohol Dehydrogenase by Methyltin Compounds
The study of inorganic tin (SnCl(2), SnCl(4)) and methyltin compounds (MeSnCl(3), Me(2)SnCI(2), Me(3)SnCl) effects on the enzymatic activity of alcohol dehydrogenase (ADH) in the reaction of ethanol oxidation has been carried out. The experimental results of the study show that inorganic tin and methyltin substances induce slight inhibition of the catalytic activity of horse liver alcohol dehyd...
متن کاملRate-limiting steps for the esterase and dehydrogenase reaction catalyzed by horse liver aldehyde dehydrogenase.
Horse liver aldehyde dehydrogenase, like other aldehyde dehydrogenases, is capable of hydrolyzing esters such as nitrophenyl acetate. Pre-steady state and burst kinetics were performed using substrate levels of enzyme to determine whether the rate-limiting step occurred prior to or after the formation of an acyl enzyme intermediate. A burst was found by both techniques for the dehydrogenase rea...
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در این پایان نامه، درهمتنیدگی بین یک سیستم نقطه کوانتومی دوگانه(مولکول نقطه کوانتومی) و میدان مورد مطالعه قرار گرفته است. از آنتروپی ون نیومن به عنوان ابزاری برای بررسی درهمتنیدگی بین اتم و میدان استفاده شده و تاثیر پارامترهای مختلف، نظیر تونل زنی(که توسط تغییر ولتاژ ایجاد می شود)، شدت میدان و نسبت دو گسیل خودبخودی بر رفتار درجه درهمتنیدگی سیستم بررسی شده اشت.با تغییر هر یک از این پارامترها، در...
15 صفحه اولstudy of cohesive devices in the textbook of english for the students of apsychology by rastegarpour
this study investigates the cohesive devices used in the textbook of english for the students of psychology. the research questions and hypotheses in the present study are based on what frequency and distribution of grammatical and lexical cohesive devices are. then, to answer the questions all grammatical and lexical cohesive devices in reading comprehension passages from 6 units of 21units th...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1955
ISSN: 0306-3283
DOI: 10.1042/bj0590097