PLASMA CLEARANCE OF GLYCOPROTEINS WITH TERMINAL MANNOSE AND N-ACETYLGLUCOSAMINE BY LIVER NON-PARENCHYMAL CELLS - STUDIES WITH BETA-GLUCURONIDASE, N-ACETYL-BETA-D-GLUCOSAMINIDASE, RIBONUCLEASE-B AND AGALACTO-OROSOMUCOID
PLASMA CLEARANCE OF GLYCOPROTEINS WITH TERMINAL MANNOSE AND N-ACETYLGLUCOSAMINE BY LIVER NON-PARENCHYMAL CELLS - STUDIES WITH BETA-GLUCURONIDASE, N-ACETYL-BETA-D-GLUCOSAMINIDASE, RIBONUCLEASE-B AND AGALACTO-OROSOMUCOID
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DOI:
10.1042/bj1760103
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发表时间:
1978-01-01
影响因子:
4.1
通讯作者:
STAHL, P
中科院分区:
文献类型:
--
作者:
SCHLESINGER, PH;DOEBBER, TW;STAHL, P
Glycoproteins having mannose and/or N-acetylglucosamine in the terminal non-reducing position and various lysosomal enzymes are rapidly cleared from plasma by the liver after i.v. administration. A [rat] liver cell-separation technique was used to determine the cellular localization of 125I-labeled .beta.-glucuronidase, RNase B, agalacto-orosomucoid and asialo-orosomucoid. On a specific radioactivity basis, all ligands except 125I-labeled asialo-orosomucoid were enriched in the non-parenchymal cell fraction. Isolated cells, fixed and stained for .beta.-glucuronidase or N-acetyl-.beta.-D-glucosaminidase activity after i.v. injection of the enzymes, showed enrichment in the non-parenchymal cell fraction (probably Kupffer cells). After uptake by the non-parenchymal cells, liver lysosomal .beta.-glucuronidase and N-acetyl-.beta.-D-glucosaminidase showed degradation half-times of 2.2 and 0.4 days respectively.