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Biochem Biophys Res Commun. 1997 Jul 9;236(1):10-5.

Purification, cloning, and expression of human plasma hyaluronidase.

Author information

1
Department of Pathology, School of Medicine, University of California, San Francisco 94143-0506, USA.

Erratum in

  • Biochem Biophys Res Commun. 2004 Jun 25;319(2):705.. Csoka, T B [corrected to Csoka, A B].

Abstract

Hyaluronidase was purified from human plasma using Triton X-114 phase extractions and ion-exchange chromatography. Monoclonal antibodies generated against the purified protein by a novel screening assay were utilized to isolate homogeneous enzyme for microsequencing. The amino acid sequences obtained matched a cDNA in the Expressed Sequence Tag database which, with 5'-RACE-PCR, was used to clone the plasma hyaluronidase gene, termed Hyal-1. Hyal-1 codes for a protein of 435 amino acids that is over 40% identical to PH-20, a sperm-specific hyaluronidase. Unlike PH-20, which is only expressed in testis, transcripts of Hyal-1 were found in multiple tissues. Hyal-1 stably expressed in human embryonic kidney cells resulted in a 3,000 fold increase of secreted immunoreactive hyaluronidase activity that was biochemically indistinguishable from human plasma hyaluronidase. By immunological, molecular and biochemical criteria, we conclude that Hyal-1 is the predominant hyaluronidase found in human plasma.

PMID:
9223416
DOI:
10.1006/bbrc.1997.6773
[Indexed for MEDLINE]

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