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Isolation of two variants of native one‐chain tissue plasminogen activator
Author(s) -
Rånby Mats,
Bergsdorf Nils,
Pohl Gunnar,
Wallén Per
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80936-8
Subject(s) - chemistry , sepharose , plasminogen activator , biochemistry , polyacrylamide gel electrophoresis , arginine , gel electrophoresis , microbiology and biotechnology , tissue plasminogen activator , chromatography , sodium , elution , enzyme , biology , amino acid , genetics , organic chemistry
The native one‐chain tissue plasminogen activator from the human melanoma cell line (Bowes) occurs in two variants as demonstrated by sodium dodecylsulphate—polyacrylamide gel electrophoresis of reduced and carboxymethylated samples. The two variants were isolated by affinity chromatography on arginine—Sepharose using a guanidinium—HCl gradient. in the order of elution, the variants were designated tissue plasminogen activator I and II. Variant I was found to be 3000 M r larger than variant II and the difference was found to reside in the N‐terminal half of the molecule. No substantial difference in carbohydrate content nor in enzymatic activity was demonstrated.