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Proteolysis of kunitz soybean trypsin inhibitor during germination

1985; Elsevier BV; Volume: 25; Issue: 1 Linguagem: Inglês

10.1016/s0031-9422(00)94494-7

1873-3700

Philippe Hartl, Anna L. Tan‐Wilson, Karl A. Wilson,

Insect Resistance and Genetics

During the germination and seedling growth of soybeans (Glycine max) a new form of the Kunitz soybean trypsin inhibitor (KSTI) appears in the cotyledons distinct from the KSTI of the quiescent seed. This inhibitor has been purified from the germinated seeds of soybean cultivar Amsoy 71 and cultivar Fiskeby V. These cultivars contain the Tia and Tii variants of KSTI respectively in the dry seed. The inhibitors were characterized by sodium dodecylsulphate-polyacrylamide gel electrophoresis, amino acid analysis, and partial sequence determination. The newly appearing form in Amsoy 71 (Tiam) was found to be identical to Tia except for the loss of the five residue sequence at the carboxylterminus of Tia. The Tib variant of KSTI was found to contain at least 199 amino acid residues (as opposed to 181 for Tia). The amino-terminal sequence of Tib was found to be identical to that of Tia for the first ten residues. The KSTI species appearing in Fiskeby V with germination, Tibm, appears to be derived from Tib by the loss of the carboxylterminal decapeptide.