Charge heterogeneity of human protein C revealed by isoelectric focusing in immobilized pH gradients

C. Gelfi, P. G. Righetti, P. M. Mannucci

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Protein C (PC), a plasma zymogen of a serine amidase with strong anticoagulant activity, has been purified to homogeneity as shown by sodium dodecyl sulfate electrophoresis. After isoelectric focusing in immobilized pH gradients, PC consists of six isobands, with isoelectric points (pI) between pH 4.8 and 5.1. That all the isobands were PC was confirmed by electroblotting on cellulose nitrate followed by immunoperoxidase staining. Activated PC gives a similar pattern of bands, with pIs ca. 0.5 units higher. Activated PC was also recognized by the monospecific antibody.

Original languageEnglish
Pages (from-to)373-376
Number of pages4
JournalElectrophoresis
Volume6
Issue number8
Publication statusPublished - 1985

Fingerprint

Proton-Motive Force
Isoelectric Focusing
Protein C
amidase
Enzyme Precursors
Collodion
Isoelectric Point
Electrophoresis
Sodium Dodecyl Sulfate
Anticoagulants
Serine
Staining and Labeling
Plasmas
Antibodies

ASJC Scopus subject areas

  • Clinical Biochemistry

Cite this

Charge heterogeneity of human protein C revealed by isoelectric focusing in immobilized pH gradients. / Gelfi, C.; Righetti, P. G.; Mannucci, P. M.

In: Electrophoresis, Vol. 6, No. 8, 1985, p. 373-376.

Research output: Contribution to journalArticle

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