Abstract
Treatment of zymogen of pancreatic-type group I phospholipase A2 (PLA2-I) by plasmin, a fibrinolytic enzyme, increases PLA2 activity as well as receptor binding activity in a dose- and time-dependent manner. Separation of plasmin-treated pro-PLA2-I by HPLC and amino acid sequence analysis of the products revealed that, in addition to an authentic mature PLA2-I produced by trypsin, plasmin produced active products which had been modified in the C-terminal region. Thus, PLA2-I may be involved in physiologic processes which accompany the formation of plasmin.
MeSH terms
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Amino Acid Sequence
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Animals
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Chromatography, High Pressure Liquid
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Enzyme Precursors / metabolism*
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Fibrinolysin / metabolism*
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Isoenzymes / metabolism*
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Kinetics
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Molecular Sequence Data
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Pancreas / enzymology
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Peptide Fragments / isolation & purification
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Phospholipases A / metabolism*
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Phospholipases A2
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Protein Precursors / metabolism*
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Receptors, Cell Surface / metabolism*
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Receptors, Phospholipase A2
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Swine
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Trypsin / metabolism
Substances
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Enzyme Precursors
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Isoenzymes
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Peptide Fragments
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Protein Precursors
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Receptors, Cell Surface
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Receptors, Phospholipase A2
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Phospholipases A
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Phospholipases A2
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prophospholipase A2
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Trypsin
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Fibrinolysin