CHARACTERIZATION OF THE MEMBRANE-PROTEINS OF RAT-LIVER LYSOSOMES - COMPOSITION, ENZYME-ACTIVITIES AND TURNOVER
CHARACTERIZATION OF THE MEMBRANE-PROTEINS OF RAT-LIVER LYSOSOMES - COMPOSITION, ENZYME-ACTIVITIES AND TURNOVER
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DOI:
10.1042/bj2040525
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发表时间:
1982-01-01
影响因子:
4.1
通讯作者:
SCHNEIDER, DL
中科院分区:
文献类型:
--
作者:
BURNSIDE, J;SCHNEIDER, DL
Lysosomes prepared from the livers of untreated rats and from the livers of rats injected with either Triton WR-1339 or dextran yielded membranes that were similar in both polypeptide composition and activities of ATPase and acid 5''-nucleotidase. The administration of Triton WR-1339 (and dextran) resulted in an increase in ATPase activity of liver homogenates that was associated with a parallel increase in the ATPase activity of the lysosomal membrane. Plasma membranes appear to be different from lysosomal membranes with respect to polypeptide composition and enzyme activities. The ATPase activity of lysosomal membranes is not affectd by ouabain and suramin, inhibitors of the plasma-membrane ATPase. The plasma-membrane alkaline 5''-nucleotidase has little activity at acid pH. Pulse-labeling of lysosomal membranes with [3H]fucose and with [3H]- and [14C]-leucine occurred rapidly, faster than labeling of plasma membranes. The labeling kinetics indicate that lysosomal membranes may be assembled independently of plasma membranes. Apparently, in liver, little bulk transport of plasma membrane to lysosomes takes place, and lysosomal-membrane proteins may not be derived from those of plasma membranes.