In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin

B.A.M. Soute; C. Vermeer; M. De Metz; H.C. Hemker; H.R. Lijnen

doi:10.1016/0304-4165(81)90013-1

In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin

B.A.M. Soute^*
, C. Vermeer
, M. De Metz
, H.C. Hemker
, H.R. Lijnen

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

Bovine descarboxyprothrombin and descarboxyfragment-1 can be used as substrates for rat and bovine vitamin K-dependent carboxylase. In both enzyme systems, these substrates have a high Km (0.3-0.4 mM). A better substrate (Km = 0.001-0.003 mM) was prepared from bovine descarboxyprothrombin by limited proteolysis with subtilisin Carlsberg. This substrate is called Fragment-Su and is composed of the amino acid 13-29 of descarboxyprothrombin.

Original language	English
Pages (from-to)	101-107
Number of pages	7
Journal	Biochimica et Biophysica Acta-general Subjects
Volume	676
Issue number	1
DOIs	https://doi.org/10.1016/0304-4165(81)90013-1
Publication status	Published - 5 Aug 1981

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Soute, B. A. M., Vermeer, C., De Metz, M., Hemker, H. C., & Lijnen, H. R. (1981). In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin. Biochimica et Biophysica Acta-general Subjects, 676(1), 101-107. https://doi.org/10.1016/0304-4165(81)90013-1

@article{2c777da56e134d119116939ecfd87b07,

title = "In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin",

abstract = "Bovine descarboxyprothrombin and descarboxyfragment-1 can be used as substrates for rat and bovine vitamin K-dependent carboxylase. In both enzyme systems, these substrates have a high Km (0.3-0.4 mM). A better substrate (Km = 0.001-0.003 mM) was prepared from bovine descarboxyprothrombin by limited proteolysis with subtilisin Carlsberg. This substrate is called Fragment-Su and is composed of the amino acid 13-29 of descarboxyprothrombin.",

author = "B.A.M. Soute and C. Vermeer and \{De Metz\}, M. and H.C. Hemker and H.R. Lijnen",

year = "1981",

month = aug,

day = "5",

doi = "10.1016/0304-4165(81)90013-1",

language = "English",

volume = "676",

pages = "101--107",

journal = "Biochimica et Biophysica Acta-general Subjects",

issn = "0304-4165",

publisher = "Elsevier B.V.",

number = "1",

}

Soute, BAM, Vermeer, C, De Metz, M, Hemker, HC & Lijnen, HR 1981, 'In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin', Biochimica et Biophysica Acta-general Subjects, vol. 676, no. 1, pp. 101-107. https://doi.org/10.1016/0304-4165(81)90013-1

In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin. / Soute, B.A.M.; Vermeer, C.; De Metz, M. et al.
In: Biochimica et Biophysica Acta-general Subjects, Vol. 676, No. 1, 05.08.1981, p. 101-107.

Research output: Contribution to journal › Article › Academic › peer-review

TY - JOUR

T1 - In vitro prothrombin synthesis from a purified precursor protein

T2 - III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin

AU - Soute, B.A.M.

AU - Vermeer, C.

AU - De Metz, M.

AU - Hemker, H.C.

AU - Lijnen, H.R.

PY - 1981/8/5

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N2 - Bovine descarboxyprothrombin and descarboxyfragment-1 can be used as substrates for rat and bovine vitamin K-dependent carboxylase. In both enzyme systems, these substrates have a high Km (0.3-0.4 mM). A better substrate (Km = 0.001-0.003 mM) was prepared from bovine descarboxyprothrombin by limited proteolysis with subtilisin Carlsberg. This substrate is called Fragment-Su and is composed of the amino acid 13-29 of descarboxyprothrombin.

AB - Bovine descarboxyprothrombin and descarboxyfragment-1 can be used as substrates for rat and bovine vitamin K-dependent carboxylase. In both enzyme systems, these substrates have a high Km (0.3-0.4 mM). A better substrate (Km = 0.001-0.003 mM) was prepared from bovine descarboxyprothrombin by limited proteolysis with subtilisin Carlsberg. This substrate is called Fragment-Su and is composed of the amino acid 13-29 of descarboxyprothrombin.

U2 - 10.1016/0304-4165(81)90013-1

DO - 10.1016/0304-4165(81)90013-1

M3 - Article

SN - 0304-4165

VL - 676

SP - 101

EP - 107

JO - Biochimica et Biophysica Acta-general Subjects

JF - Biochimica et Biophysica Acta-general Subjects

IS - 1

ER -

In vitro prothrombin synthesis from a purified precursor protein: III. Preparation of an acid-soluble substrate for vitamin K-dependent carboxylase by limited proteolysis of bovine descarboxyprothrombin

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