Differences between uterine and melanoma forms of tissue plasminogen activator |
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Authors: | Gunnar Pohl Lennart Kaplan Monica Einarsson Per Wallén Hans Jörnvall |
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Affiliation: | Department of Physiological Chemistry, Umeå University, S-90187 Umeå, Kabi Vitrum, S-11287 Stockholm, Sweden;Department of Chemistry I, Karolinska Institutet, S-104 01 Stockholm, Sweden |
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Abstract: | Tissue plasminogen activator purified from human uterine tissue exhibits differences in N-terminal starting positions in relation to the melanoma cell plasminogen activator usually studied. A new starting position is compatible with an additional N-terminal processing apart from those already known. Like the melanoma activator, the uterine activator was found to yield protein chains starting at either of two positions. One of these was identical between uterine and melanoma activators, whereas the other was unique in each case. The most abundant starting position for the uterine preparation was at a valine residue, apparently from cleavage of a Gln-Val bond, and corresponding to Val-7 of the longest form of the melanoma activator chain. |
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Keywords: | Amino acid sequence analysis N-terminal proteolysis Protein processing t-PA tissue-type plasminogen activator |
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