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pro vyhledávání: '"S G, Nerurkar"'
Autor:
K K, Gambhir, S G, Nerurkar
Publikováno v:
Biochemistry international. 23(2)
Internalization and degradation of insulin by human erythrocytes were studied. Erythrocytes were incubated with 125I-insulin at 4 degrees C, 15 degrees C, and 37 degrees C for varying time intervals. These erythrocytes were then subjected to a low pH
Autor:
K. K. Gambhir, S G Nerurkar
Publikováno v:
Clinical Chemistry. 27:607-609
In vitro hemolysates of isolated human erythrocytes degrade 125I-labeled insulin. Ten- to 100-fold dilutions of the hemolysate give a proportionately decreased degradation of 125I-labeled insulin at 37 degrees C, while dilutions of up to eightfold do
Autor:
S. G. Nerurkar, Kanwal K. Gambhir
Publikováno v:
Diabetologia. 26
Publikováno v:
Journal of submicroscopic cytology. 18(4)
In estrogen and diethylstilbestrol-treated rats, uterine peroxidases originate from two sources, the infiltrating eosinophils (exogenous) and the uterine tissue itself (endogenous). The study reported here distinguished the exogenous peroxidases by b
Autor:
S G, Nerurkar, K K, Gambhir
Publikováno v:
Clinical chemistry. 27(4)
In vitro hemolysates of isolated human erythrocytes degrade 125I-labeled insulin. Ten- to 100-fold dilutions of the hemolysate give a proportionately decreased degradation of 125I-labeled insulin at 37 degrees C, while dilutions of up to eightfold do
Publikováno v:
Endocrinology. 109(5)
When evaluated at 15 C, insulin binding to human erythrocytes is similar to that of human adipocytes fibroblasts, monocytes and placental membranes. At 37 C, however, both insulin binding and degradation by human erythrocytes have a unique character.
Autor:
K. K. Gambhir, S G Nerurkar
Publikováno v:
Clinical Chemistry. 25:1672-1673