PURIFICATION AND IMMUNOHISTOCHEMICAL STUDY OF SORBITOL DEHYDROGENASE IN RAT LIVER
نویسندگان
چکیده
منابع مشابه
Purification and properties of dihydrothymine dehydrogenase from rat liver.
Rat liver dihydrothymine dehydrogenase, the rate-limiting enzyme of thymidine and uridine degradation, was purified to homogeneity as judged by polyacrylamide disc gel electrophoresis, sedimentation velocity, and Ultrogel ACA-34 elution profile. The enzyme has a molecular weight of 220,000 +/- 5,000 as determined by Ultrogel ACA-34 and sedimentation equilibrium The s20,w value of the enzyme was...
متن کاملSynthesis 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 کاملPurification and characterization of methylmalonate-semialdehyde dehydrogenase from rat liver. Identity to malonate-semialdehyde dehydrogenase.
Methylmalonate semialdehyde dehydrogenase was purified from rat liver in order to define the distal portion of valine catabolism and related pathways in mammals. The purified enzyme is active with malonate semialdehyde and consumes both stereoisomers of methylmalonate semialdehyde, implicating a single semialdehyde dehydrogenase in the catabolism of valine, thymine, and compounds catabolized by...
متن کاملa contrastive study of rhetorical functions of citation in iranian and international elt scopus journals
writing an academic article requires the researchers to provide support for their works by learning how to cite the works of others. various studies regarding the analysis of citation in m.a theses have been done, while little work has been done on comparison of citations among elt scopus journal articles, and so the dearth of research in this area demands for further investigation into citatio...
Rat 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 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: ACTA HISTOCHEMICA ET CYTOCHEMICA
سال: 1976
ISSN: 0044-5991,1347-5800
DOI: 10.1267/ahc.9.144