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Plasma prekallikrein: Isolation, characterization, and mechanism of activation

Academic Article
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Overview

authors

  • Wuepper, K. D.
  • Cochrane, Charles

publication date

  • 1972

journal

  • Journal of Experimental Medicine  Journal

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.

subject areas

  • Amino Acids
  • Animals
  • Aprotinin
  • Blood Proteins
  • Chromatography, Gel
  • Chromatography, Ion Exchange
  • Electrophoresis, Disc
  • Enzyme Activation
  • Enzyme Precursors
  • Glycoproteins
  • Humans
  • Hydrolysis
  • Iodine Isotopes
  • Isoelectric Focusing
  • Kallikreins
  • Methods
  • Molecular Weight
  • Rabbits
  • Species Specificity
  • Trypsin
  • Ultracentrifugation
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Identity

PubMed Central ID

  • PMC2139124

International Standard Serial Number (ISSN)

  • 0022-1007

Digital Object Identifier (DOI)

  • 10.1084/jem.135.1.1

PubMed ID

  • 4536682
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Additional Document Info

start page

  • 1

end page

  • 20

volume

  • 135

issue

  • 1

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