INVITRO ASSESSMENT OF TC-99M LABELED BOVINE THROMBIN AND STREPTOKINASE-ACTIVATED HUMAN PLASMIN - CONCISE COMMUNICATION
- 1 January 1979
- journal article
- research article
- Vol. 20 (9) , 967-972
Abstract
Bovine thrombin and streptokinase-activated human plasmin were labeled with Tc-99m using stannous pertechnetate reduction under physiological conditions (pH 7.4). Binding efficiency of radioTc to these enzymes was greater than 94%, with less than 5% of reduced but unbound Tc-99m (Sn) complex as assayed by ascending paper radiochromatography using ITLC [instant TLC] silica gel plate. Free or unbound pertechnetate was less than 1%. In vitro enzymatic analyses of Tc-99m-labeled enzymes demonstrate no evidence of protein denaturation or significant enzymatic activity loss after labeling. Both labeled enzymes were biochemically active in vitro with their respective substrates.This publication has 5 references indexed in Scilit:
- A rapid chemical method of labeling human plasma proteins with 99mTc-pertechnetate at pH 7.4The International Journal of Applied Radiation and Isotopes, 1978
- Mechanism of activation of human plasminogen by the activator complex, streptokinase-plasminJournal of Biological Chemistry, 1978
- Protease inhibitors and human plasmin: Interaction in a whole plasma systemBiochemical and Biophysical Research Communications, 1977
- Labeling plasmin with technetium-99m for scintigraphic localization of thrombiThe International Journal of Applied Radiation and Isotopes, 1977
- THE MECHANISM OF CLOT DISSOLUTION BY PLASMIN*Journal of Clinical Investigation, 1959