Studies on rat-liver glycylglycine dipeptidase
نویسندگان
چکیده
منابع مشابه
Dipeptidase deficiency and malabsorption of glycylglycine in disease states.
The activities of jejunal mucosal peptide hydrolases for glycylglycine, glycyl-L-leucine and L-leucylglycine, were assayed in 37 patients. Eight patients, four of whom had Crohn's disease, were found to have a marked reduction in the activity of glycylglycine dipeptidase and, to a lesser extent, of the other two hydrolases. Although absorption of glycine in the two groups was similar, there was...
متن کاملStudies on Dipeptidases Iii , Hydrolysis of Methylated Peptides; the Role of Cobalt in the Action of Glycylglycine Dipeptidase* by Emil
The recognition that the hydrolysis of the peptides, glycylglycine and glycyl-n-leucine, is due to specific dipeptidases (l-3) has led to a search for an explanation of why the responsible enzymes should require such extremely specific substrate configurations. While a complete description is obviously not yet possible, a partial answer seems to be in the role that certain metals play in these ...
متن کاملStudies on Squalene Epoxidase of Rat Liver*
Rat liver microsomes previously heated to 50” for 5 mm accumulate 2,3-oxidosqualene on incubation with squalene. Squalene epoxidase activity can be assayed either with squalene and heated microsomes or with lO,ll-dihydrosqualene and intact microsomes. In common with other monooxygenases, the epoxidase requires TPNH and molecular oxygen. Both a soluble fraction of rat liver and microsomes are ne...
متن کاملStudies on squalene epoxidase of rat liver.
Rat liver microsomes previously heated to 50” for 5 mm accumulate 2,3-oxidosqualene on incubation with squalene. Squalene epoxidase activity can be assayed either with squalene and heated microsomes or with lO,ll-dihydrosqualene and intact microsomes. In common with other monooxygenases, the epoxidase requires TPNH and molecular oxygen. Both a soluble fraction of rat liver and microsomes are ne...
متن کاملTurnover studies on proteins of rat liver lysosomes.
The turnover of rat liver lysosomal proteins was studied by a double isotope-labeling technique. The cellular fractions investigated included soluble lysosomal proteins, lysosomal membrane proteins, highly purified lysosomal beta-glucuronidase, and for comparison, microsomal proteins and soluble cytoplasmic proteins. Both "normal" lysosomes and Triton WR-1339-filled lysosomes (tritosomes) were ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1963
ISSN: 0006-2936
DOI: 10.1042/bj0870192