[Isolation of a specific inhibitor of microbial serine proteinase from kidney bean seeds]. / Vydelenie iz semian fasoli spetsificheskogo ingibitora serinovykh proteinaz mikroorganizmov.

A protein acting as a specific inhibitor of microbial serine proteinases was isolated from kidney bean seeds. The purification procedure included complex formation between the inhibitor and Aspergillus oryzae proteinase. The protein with a Mr approximately 10 000 inhibits subtilisin and Asp. oryzae proteinase but does not affect trypsin and chymotrypsin. The inhibitor molecule contains no half-cystine residues.

[Identification of the reactive sites of kidney bean proteinase inhibitor]. / Stroenie reaktivnykh tsentrov belka - ingibitora serinovykh proteinaz iz fasoli.

The protein proteinase inhibitor from kidney bean (isoinhibitor, pI 4.3) is a double-headed inhibitor with independent reactive sites for trypsin and chymotrypsin. The reactive site of the inhibitor for trypsin is Lys (22)- Ser (23) in the sequense ...-Lys-Ser-Ile-Pro-Ala-Glx-Cys-Arg-..., the reactive site for chymotrypsin is Leu (64)-Ser (65) in the sequence ...-Thr-Leu-Ser-Ile-Pro-Ala-Glx-Cys-Arg-... .

[Comparative study of preparations of hirudin and "pseudohirudin"]. / Sravintel'noe izuchenie girudina i "psevdogirudina".

In contrast to hirudin, "pseudohirudin", which is practically devoid of the antithrombin activity, is represented as associates of di- and trimers. The molecular weight of the "pseudohirudin" monomer is by 2000 less than that for hirudin. This corresponds to the 20 amino acid residues difference calculated from the total number of the amino acid residues. Changes in the amino acid composition consist in a higher content of dicarboxylic amino acids, isoleucine, lysine, tyrosine and cystein in the hirudin preparations.

A specific inhibitor of Colletotrichum lindemuthianum protease from kidney bean (Phaseolus vulgaris) seeds.

A specific protein-an inhibitor of Colletotrichum lindemuthianum protease-was isolated from kidney bean seeds in a homogeneous form. The purification procedure included gel filtration, isoelectric focusing and affinity chromatography on trypsin-Sepharose column. The latter was introduced to separate the fungal protease inhibitor from closely related trypsin and chymotrypsin inhibitors present in kidney bean seeds.

[Physico-chemical properties of a protein-inhibitor of serine proteinases from the potato]. / Izuchenie fiziko-khimicheskikh svoistv belka--inhibitora serinovykh proteinaz iz kartofelia

Serine proteases inhibitor with pl-7.3, isolated from potatoe tubers by isoelectric focusing procedure as described previously (V.V. Mosolov et al., Bioorganic Chem., 1, 1449, 1975), was homogeneous under ultracentrifugation, having sedimentation coefficient S20,w 2.8S. Its molecular weight, investigated by sedimentation equilibrium and gel filtration through Sephadex G-100, was found to be 32500 and 31500 respectively. The Stokes radius R and frictional ratio f/fo were found to be 24 A and 1.14. The molecular weight of the inhibitor as determined by sodium dodecylsulfate polyacrylamide electrophoresis was twice as low as determined in ultracentrifuge and by gel filtration procedure. It is suggested that the inhibitor is dimer and consists of two protomers of equal molecular weight.