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Uptake of l ‐[ 35 S]Cystine by Isolated Rat Brain Capillaries
Author(s) -
Hwang Shing Mei,
Weiss Steven,
Segal Stanton
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb06281.x
Subject(s) - cystine , chemistry , biochemistry , neuroscience , biology , cysteine , enzyme
Adult rat brain capillaries were isolated by a simplified procedure and showed an enrichment of the marker enzyme, γ‐glutamyltranspeptidase. The uptake of [ 35 S]cystine at 37°C by this preparation can be divided into two components, a sodium‐ and energy‐dependent transport process for the free amino acid pool, with an apparent K m of 36 μ m , and a binding process, with an apparent K m of 1.13 m m . Chemical analysis of the amino acid pool indicates that cystine is the major form of intracapillary 35 S. Cystine transport was not inhibited by lysine, but glycine, α‐methylaminoisobutyric acid and β‐2‐aminobicyclo‐[2,2,1]‐heptane‐2‐carboxylic acid were inhibitory to a small extent.