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Differential proteolysis and evidence for a residue exchange in tissue plasminogen activator suggest possible association between two types of protein microheterogeneity
Author(s) -
Jörnvall Hans,
Pohl Gunnar,
Bergsdorf Nils,
Wallén Per
Publication year - 1983
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(83)80245-2
Subject(s) - proteolysis , residue (chemistry) , plasminogen activator , chemistry , biochemistry , plasmin , activator (genetics) , biology , enzyme , endocrinology , receptor
The N‐terminal part of native one‐chain tissue plasminogen activator from melanoma cells is not homogeneous. The protein chain starts at two different postions, in all probability representing a processing difference in the N‐terminus. Both ‘long’ L‐chains and 3‐residue shorter S‐chains are present in the preparations. In addition, results compatible with a positional Ser/Gly microheterogeneity were obtained at a single position (positions L‐4 which is equal to S‐1). The N‐terminal tripeptide difference seems to be coupled to the possible microheterogeneity: L‐chains contain Ser in this position, while S‐chains appear to contain predominantly Gly.