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Thrombokinase of the Blood as Trypsin-Like Enzyme
Thrombokinase of the blood, while resembling enterokinase in its role of activator, is more closely analogous to trypsin in its intrinsic origin. It probably arises from a plasma precursor; but it is different from plasmin (fibrinolysin). Like trypsin, thrombokinase can activate prothrombin without...
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Formato: | Texto |
Lenguaje: | English |
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The Rockefeller University Press
1962
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195203/ https://www.ncbi.nlm.nih.gov/pubmed/14035995 |
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author | Milstone, J. H. |
author_facet | Milstone, J. H. |
author_sort | Milstone, J. H. |
collection | PubMed |
description | Thrombokinase of the blood, while resembling enterokinase in its role of activator, is more closely analogous to trypsin in its intrinsic origin. It probably arises from a plasma precursor; but it is different from plasmin (fibrinolysin). Like trypsin, thrombokinase can activate prothrombin without the aid of other factors; however, it is potentiated by platelets plus calcium. Unlike certain tissue "thromboplastins," it does not sediment appreciably in 2 hours at 85,000 g. Like trypsin, it hydrolyzes p-toluenesulfonylarginine methyl ester (TAMe). Chromatography on DEAE-cellulose separated thrombin from thrombokinase. The TAMe esterase associated with the thrombokinase fractions was largely suppressed by soybean trypsin inhibitor, while that associated with the thrombin fractions was not. Highly purified thrombokinase was used as starting material; and thrombokinase was eluted in the last major protein band. Under these conditions stepwise elution was as effective as gradient in leading to further purification. The product of 199 liters of bovine plasma was chromatographed in 1 day; and the specific activity was comparable to that attained previously by repeated electrophoretic fractionations. The assembled data suggest that the thrombokinase protein may be approaching homogeneity. |
format | Text |
id | pubmed-2195203 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1962 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21952032008-04-23 Thrombokinase of the Blood as Trypsin-Like Enzyme Milstone, J. H. J Gen Physiol Article Thrombokinase of the blood, while resembling enterokinase in its role of activator, is more closely analogous to trypsin in its intrinsic origin. It probably arises from a plasma precursor; but it is different from plasmin (fibrinolysin). Like trypsin, thrombokinase can activate prothrombin without the aid of other factors; however, it is potentiated by platelets plus calcium. Unlike certain tissue "thromboplastins," it does not sediment appreciably in 2 hours at 85,000 g. Like trypsin, it hydrolyzes p-toluenesulfonylarginine methyl ester (TAMe). Chromatography on DEAE-cellulose separated thrombin from thrombokinase. The TAMe esterase associated with the thrombokinase fractions was largely suppressed by soybean trypsin inhibitor, while that associated with the thrombin fractions was not. Highly purified thrombokinase was used as starting material; and thrombokinase was eluted in the last major protein band. Under these conditions stepwise elution was as effective as gradient in leading to further purification. The product of 199 liters of bovine plasma was chromatographed in 1 day; and the specific activity was comparable to that attained previously by repeated electrophoretic fractionations. The assembled data suggest that the thrombokinase protein may be approaching homogeneity. The Rockefeller University Press 1962-03-01 /pmc/articles/PMC2195203/ /pubmed/14035995 Text en Copyright © Copyright, 1962, by The Rockefeller Institute Press. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Article Milstone, J. H. Thrombokinase of the Blood as Trypsin-Like Enzyme |
title | Thrombokinase of the Blood as Trypsin-Like Enzyme |
title_full | Thrombokinase of the Blood as Trypsin-Like Enzyme |
title_fullStr | Thrombokinase of the Blood as Trypsin-Like Enzyme |
title_full_unstemmed | Thrombokinase of the Blood as Trypsin-Like Enzyme |
title_short | Thrombokinase of the Blood as Trypsin-Like Enzyme |
title_sort | thrombokinase of the blood as trypsin-like enzyme |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2195203/ https://www.ncbi.nlm.nih.gov/pubmed/14035995 |
work_keys_str_mv | AT milstonejh thrombokinaseofthebloodastrypsinlikeenzyme |