Characterization Studies on Human Melanoma Cell Tissue Plasminogen Activator View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-12

AUTHORS

Gordon A. Vehar, William J. Kohr, William F. Bennett, Diane Pennica, Carole A. Ward, Richard N. Harkins, Desire Collen

ABSTRACT

Purified tissue plasminogen activator synthesized by a human melanoma cell line has been partially characterized. On SDS gel electrophoresis, the purified samples exhibited a doublet at molecular weights 63,000 and 65,000. Staphylococcal V8 proteolytic digestion of the separated species yielded similar size fragments, indicating gross identity of the polypeptide chains. It was subsequently found that these species had differential binding to lysine-Sepharose, with the lower apparent molecular weight species binding with a higher affinity. Amino acid sequence determination of reverse phase HPLC tryptic fragments has resulted in the characterization of approximately 80 percent of the protein. The identification of a cDNA clone has allowed alignment of these tryptic peptides. The molecule was found to be composed of an amino terminal domain, two kringle structures, and a serine protease. The molecule is composed of 527 amino acids, and has potential glycosylation sites at asparagine positions 117, 184, 218, and 448. The peptide containing Asn 448 was sequenced and determined to be glycosylated, whereas a peptide containing Asn-218 was found not to be glycosylated. Comparison of the kringle and serine protease domains with other serine proteases is discussed. More... »

PAGES

1051

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nbt1284-1051

DOI

http://dx.doi.org/10.1038/nbt1284-1051

DIMENSIONS

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