Plasma prekallikrein: isolation, characterization, and mechanism of activation.

The Journal of experimental medicine ·Vol. 135 ·No. 1 ·1972-01-00 ·Pages 1-20

Wuepper KD, Cochrane CG

Abstract

The precursor of the kinin-forming enzyme, prekallikrein, was isolated from rabbit plasma protected from activation during preparatory procedures. Prekallikrein was shown to be a 4.5S gamma(1)-glycoprotein with an isoelectric point of 5.9 and a mol wt of 99,900. The proenzyme was activated at neutral pH by an enzyme from rabbit or human plasma we have termed prekallikrein activator (PKA) or by trypsin. Prekallikrein was activated by PKA by a process of enzymatic scission. This resulted in the appearance of two fragments; the larger of these possessed kallikrein activity.

MeSH Terms

Amino Acids Animals Aprotinin/pharmacology Blood Proteins Chromatography, Gel Chromatography, Ion Exchange Electrophoresis, Disc Enzyme Activation Enzyme Precursors/analysis,blood,isolation & purification,pharmacology Glycoproteins/isolation & purification Humans Hydrolysis Iodine Isotopes Isoelectric Focusing Kallikreins/blood,isolation & purification Methods Molecular Weight Rabbits Species Specificity Trypsin/pharmacology Ultracentrifugation

Chemicals

Amino Acids Blood Proteins Enzyme Precursors Glycoproteins Iodine Isotopes Aprotinin Kallikreins Trypsin

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Wuepper K D

Cochrane C G

References (18)

18 references, click to expand

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Article Info

Journal

The Journal of experimental medicine

Abbr.

J Exp Med

ISSN

0022-1007

DOI

10.1084/jem.135.1.1

Published

1972-01-00

Pages

1-20

Language

English

Region

United States

NLM ID

2985109R

PMCID

PMC2139124

Subset

External Links

PubMed source DOI: 10.1084/jem.135.1.1 PMC Full Text View journal details

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Plasma prekallikrein: isolation, characterization, and mechanism of activation.

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