منابع مشابه
Synthesis and Degradation of Rat Liver Lactate Dehydrogenase M4 HYBRIDIZATION IN THE PURIFICATION OF LACTATE DEHYDROGENASE
For the measurement of lactate dehydrogenase (LDH) isoenzyme biosynthesis a new method is presented which is based on the quantitative hybridization of isoenzyme MI with isoenzyme Hq. After reversible dissociation the formation of active LDH M4 was more rapid and occurred to a greater extent than the formation of LDH Hq. The formation of hybrid isoenzymes from the two subunits resulted in an in...
متن کاملSynthesis and degradation of rat liver lactate dehydrogenase M4. Hybridization in the purification of lactate dehydrogenase isoenzymes.
For the measurement of lactate dehydrogenase (LDH) isoenzyme biosynthesis a new method is presented which is based on the quantitative hybridization of isoenzyme MI with isoenzyme Hq. After reversible dissociation the formation of active LDH M4 was more rapid and occurred to a greater extent than the formation of LDH Hq. The formation of hybrid isoenzymes from the two subunits resulted in an in...
متن کاملRat Liver Aldehyde Dehydrogenase
From normal rat liver mitochondrial and microsomal fractions, 4 distinct aldehyde dehydrogenase isozymes with millimolar substrate K,,, values have been purified and characterized. Two isozymes were isolated from mitochondria and 2 from microsomes. A mitochondrial aldehyde dehydrogenase with a substrate K,,, in the micromolar range was also identified. Subunit molecular weights for all millimol...
متن کاملVARIATIONS BY EPINEPHRINE OF HEPATIC AND SERUM AMINOTRANSFERASES AND LACTATE DEHYDROGENASE IN THE RAT
Incubation of rat hepatocytes with epinephrine inhibited alanine aminotransferase (ALT) (80%) and aspartate aminotransferase (AST) (53%) activities with no effect on lactate dehydrogenase (LDH) activity. Injection of epinephrine caused a progressive increase with time in hepatic LDH activity, being 52% at 24 h. Preinjection with propranolol eliminated the hormone effect and caused further ...
متن کاملRat liver L-threonine dehydrogenase.
L-threonine dehydrogenase (E.C.1.1.1.103) catalyzes the NAD+-dependent transformation of Lthreonine to 2-amino 3-0x0-butyric acid, which spontaneously loses CO2 with the final production of aminoacetone ( 1) The enzyme is present in several microorganisms as well as in the liver of vertebrates (2-6). We studied some properties of the rat liver enzyme, showing that the activity was strongly inhi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)99653-5