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Twelve amino acid sequences of kringle-forming polypeptides were compiled from the known sequences of urokinase A-chain (human), a tissue-type plasminogen activator (human), prothrombin (human and bovine), and plasminogen (human). Their sequence homologies with maximum match were examined by a computer program. A homology alignment and graphic matrix analyses did show that they had a great degree of homology. All the cystein residues responsible for the kringle structures of urokinase and thedoi:10.1247/csf.10.209 fatcat:dwl4unwyc5bofhbfhmswj26pxq