Zobrazeno 1 - 10
of 41
pro vyhledávání: '"Partab T. Varandani"'
Publikováno v:
Experimental Biology and Medicine. 156:123-126
SummaryThe phospholipid composition of livers obtained from obese-hyperglycemic (ob/ob) male mice and from their lean mates was compared. In unfractionated liver ho-mogenates, the content (percentage of the total lipid phosphorus) of phosphatidyl-cho
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 538:343-353
The distribution of glutathione-insulin transhydrogenase (glutathione: protein-disulphide oxidoreductase, EC 1.8.4.2) in isolated rat hepatocytes that had been first treated with rabbit antiserum against purified rat liver transhydrogenase and then w
Autor:
Partab T. Varandani, Lois A. Shroyer
Publikováno v:
Archives of Biochemistry and Biophysics. 236:205-219
A thiol peptidase that catalyzes at near neutral pH the hydrolysis of insulin, the isolated A and B chains of insulin, and glucagon was purified from rat liver cytosol by fractionation on Sephadex G-200, Affi-Gel Blue, and Spherogel TSK-G 3000 SW. Th
Insulin Degradation: IX. On the Presence of Glutathione-insulin Transhydrogenase in Human Leukocytes
Publikováno v:
Diabetes. 23:232-239
The occurrence of insulin-degrading activity in the components of human blood has been studied. Leukocytes have been found to contain such activity. On the basis of activation by reduced glutathione, complete inhibition by N-ethyl-maleimide, kinetic
Autor:
Partab T. Varandani
Publikováno v:
Biochemical and Biophysical Research Communications. 60:1119-1126
Islet cell tumors (insulinomas) have been found to contain insulin-degrading activity. Apparent K m values for insulin obtained with tumor extracts were similar to those found for other tissues and for purified glutatione-insulin transhydrogenase (GI
Autor:
Partab T. Varandani, Mary Ann Nafz
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 870:502-509
A partially purified insulin receptor preparation from rat liver was incubated at 37 degrees C with and without the protein-disulfide interchange enzyme, glutathione-insulin transhydrogenase (thiol: protein-disulfide oxidoreductase/isomerase, EC 1.8.
Publikováno v:
Archives of Biochemistry and Biophysics. 254:35-42
The activity of the insulin-degrading enzyme neutral cysteine proteinase (EC 3.4.22.11, insulinase) was studied in adipose tissue and in liver of nondiabetic, streptozotocindiabetic, and insulin-treated diabetic rats. Proteinase activity was found to
Autor:
Eugene P. Hern, Partab T. Varandani
Publikováno v:
Biochemical and Biophysical Research Communications. 116:909-915
Summary We have studied glutathione-insulin transhydrogenase (GIT) activity in differentiating rat liver during parturition and neonatal growth and during compensatory liver growth. Parturition is characterized by a rapid but transient increase in to
Autor:
Partab T. Varandani, Mary Ann Nafz
Publikováno v:
Diabetes. 25:173-179
Isolated liver cells contain insulin-degrading activity. Examination by chromatography on Sephadex G-75 of the products formed from 125I-insulin (1 nM or 1 µM) upon incubation with suspensions of hepatocytes for various time periods showed that ther
Publikováno v:
Biochemistry. 14:2107-2115
Kinetic studies have been made with glutathione-insulin transhydrogenase, an enzyme which degrades insulin by promoting cleavage of its disulfide bonds via sulfhydryl-disulfide interchange. The degradation of 125I-labeled insulin by enzyme purified f