Selective Phagocytosis: A New Concept in Protein Catabolism
- 5 January 1968
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 159 (3810) , 107-110
- https://doi.org/10.1126/science.159.3810.107
Abstract
The clearance of different metabolic products derived from two plasma proteins, prothrombin and fibrinogen, was studied with the aid of the isolated, perfused rat liver. Active thrombin and fibrin were rapidly cleared by the Kupffer cells. Inactive thrombin and a partially degraded fibrin molecule were also cleared but at much slower rates. This difference in clearance rates suggests the presence of a high degree of selectivity in the clearance of altered plasma proteins.This publication has 12 references indexed in Scilit:
- Activation of Trypsinogen and Plasminogen by Thrombin Preparations*Biochemistry, 1966
- Study of mechanisms which preserve blood fluidity and the effect of their inhibition on thrombogenesisJournal of Surgical Research, 1966
- IN VIVO BEHAVIOR OF I131-FIBRINOGENJournal of Clinical Investigation, 1963
- Isolation of Human Thrombin.Experimental Biology and Medicine, 1962
- Sites of plasma albumin catabolism in the ratAmerican Journal of Physiology-Legacy Content, 1961
- Labeled DIP-thrombinBiochimica et Biophysica Acta, 1958
- The use of the isolated perfused liver to detect alterations to plasma proteinsBiochemical Journal, 1957
- Circulatory Pathways in the Rat Liver as Revealed by P32 Chromic Phosphate Colloid Uptake in the Isolated Perfused Liver PreparationAmerican Journal of Physiology-Legacy Content, 1956
- THE INFLUENCE OF HEPARIN ON THE ACTIVATION ENERGY OF THROMBIN INACTIVATIONCanadian Journal of Medical Sciences, 1952
- A Quantitative Study of the Fibrinolysin-Antifibrinolysin ReactionScience, 1945