Protein inhibitors of microbial proteinases from wheat, rye and triticale

• Published in: Planta Vol. 167; no. 4; pp. 595 - 600
• Main Authors: Mosolov, V.V. (A.N. Bach Inst. of Biochemistry, Moscow (USSR)), Shul'gin, M.N
• Format: Journal Article
• Language: English
• Published: Berlin Springer-Verlag 01-04-1986; Springer
• Subjects: Agronomy. Soil science and plant productions; Analytical, structural and metabolic biochemistry; ASPERGILLUS; Barley; Biological and medical sciences; Chromatography; Economic plant physiology; Electrophoresis; ENFERMEDADES FUNGOSAS; Enzymes; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Gels; Gewebe; Hemmung; HIDROLASAS; Hydrogen; HYDROLASE; HYDROLASES; Inhaltsstoffanalyse; MYCOSE; MYCOSES; Nutrition. Photosynthesis. Respiration. Metabolism; Peroxides; Pilzenzym; PROTEINAS; proteinase inhibitor; PROTEINE; Proteinhemmstoff; PROTEINS; Rye; Secale; SECALE CEREALE; Subtilisin; TRITICALE; TRITICALES; Triticum; TRITICUM AESTIVUM; Ungulates; Protein inhibitor; Monocotyledones; Microbial serine proteinases; Vegetals; Secale cereale; Gramineae; Proteinase; Angiospermae; Triticale; Spermatophyta; Serine proteinase; Triticum aestivum
• ISSN: 0032-0935; 1432-2048
• DOI: 10.1007/BF00391238

Specific protein inhibitors of microbial serine proteinases were isolated from wheat (Triticum aestivum L.), rye (Secale cereale L.) and triticale using affinity chromatography on subtilisin-Sepharose 4B. The wheat inhibitor had an isoelectric point (pI) at pH 7.2, while the rye inhibitor consisted of two forms with pI values of 6.8 and 7.1. In triticale, two components were present with pIs 7.2 and 6.8. All the inhibitors had Mr values of approx. 20000. The isolated proteins were effective inhibitors of subtilisins Carlsberg and BPN′, and of fungal proteinases (EC 3.4.21.14) from the genus Aspergillus, but they were completely inactive against trypsin (EC 3.4.21.4) chymotrypsin (EC 3.4.21.1) and pancreatic elastase (EC 3.4.21.36). The inhibitors formed complexes with subtilisin in a molar ratio of 1:1. The results of chemical modifications seem to indicate that the isolated inhibitors have methionine residues in their reactive sites.