Isolation and amino acid sequence of a cystatin-type cysteine proteinase inhibitor from bovine hoof

1996 ◽  
Vol 288 (8) ◽  
pp. 484-488
Author(s):  
H. Tsushima ◽  
Kayo Higashiyama ◽  
Hiroko Mine
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor ◽  
Bovine Hoof

scholarly journals Complete amino acid sequence of bovine colostrum low-M r cysteine proteinase inhibitor

FEBS Letters ◽  
1985 ◽  
Vol 186 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Masayuki Hirado ◽  
Susumu Tsunasawa ◽  
Fumio Sakiyama ◽  
Michio Niinobe ◽  
Setsuro Fujii
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteinase Inhibitor ◽  
Cysteine Proteinase ◽  
Bovine Colostrum ◽  
Cysteine Proteinase Inhibitor ◽  
Complete Amino Acid Sequence

scholarly journals Mammalian protein methylesterase. Physical and enzymic properties

1989 ◽  
Vol 260 (1) ◽  
pp. 11-17 ◽  
Author(s):  
K Veeraragavan ◽  
C Gagnon
Keyword(s):  
Amino Acid ◽  
Proteinase Inhibitor ◽  
Adrenocorticotropic Hormone ◽  
Cysteine Proteinase ◽  
Methyl Groups ◽  
Cysteine Proteinase Inhibitor ◽  
Amino Acid Residues ◽  
Protein Substrates ◽  
Order Of Magnitude ◽  
Mammalian Protein

Protein methylesterase (PME) amino acid composition and substrate specificity towards methylated normal and deamidated protein substrates were investigated. The enzyme contained 23% acidic and 5% basic residues. These values are consistent with a pI of 4.45. The product formed from methylated protein by PME was confirmed as methanol by h.p.l.c. The kcat. and Km values for several methylated protein substrates ranged from 20 x 10(-6) to 560 x 10(-6) s-1 and from 0.5 to 64 microM respectively. However, the kcat./Km ratios ranged within one order of magnitude from 11 to 52 M-1.s-1. Results with the irreversible cysteine-proteinase inhibitor E-64 suggested that these low values were in part due to the fact that only one out of 25 molecules in the PME preparations was enzymically active. When PME was incubated with methylated normal and deamidated calmodulin, the enzyme hydrolysed the latter substrate at a higher rate. The Km and kcat. for methylated normal calmodulin were 0.9 microM and 31 x 10(-6) s-1, whereas for methylated deamidated calmodulin values of 1.6 microM and 188 x 10(-6) s-1 were obtained. The kcat./Km ratios for methylated normal and deamidated calmodulin were 34 and 118 M-1.s-1 respectively. By contrast, results with methylated adrenocorticotropic hormone (ACTH) substrates indicated that the main difference between native and deamidated substrates resides in the Km rather than the kcat. The Km for methylated deamidated ACTH was 5-fold lower than that for methylated native ACTH. The kcat./Km ratios for methylated normal and deamidated ACTH were 43 and 185 M-1.s-1 respectively. These results indicate that PME recognizes native and deamidated methylated substrates as two different entities. This suggests that the methyl groups on native calmodulin and ACTH substrates may not be on the same amino acid residues as those on deamidated calmodulin and ACTH substrates.

scholarly journals Purification and characterization of a new cystatin inhibitor from Taiwan cobra (Naja naja atra) venom

1998 ◽  
Vol 331 (1) ◽  
pp. 239-244 ◽  
Author(s):  
Michèle BRILLARD-BOURDET ◽  
Vinh NGUYÊN ◽  
Michèle FERRER-DI MARTINO ◽  
Francis GAUTHIER ◽  
Thierry MOREAU
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cysteine Proteinase ◽  
Cathepsin L ◽  
Cysteine Proteinase Inhibitor ◽  
Naja Naja ◽  
Cystatin M ◽  
Human Cystatin ◽  
Naja Atra

Cobra cystatin, a new cysteine-proteinase inhibitor of the cystatin superfamily, was isolated from the venom of the Taiwan cobra (Naja naja atra) by affinity chromatography on S-carboxymethylpapain–Sepharose and reverse-phase chromatography. The venom contained two forms of the inhibitor, one of 11870 Da and the other of 12095 Da, as determined by MS, and pI values of 6.2 and 6.1. Cobra cystatin strongly inhibits cysteine proteinases of the papain family, but not calpain. Papain, cathepsin L, cathepsin B and cathepsin S are inhibited with Ki values of 0.19, 0.1, 2.5 and 1.2 nM respectively. The amino acid sequence of cobra cystatin shows that it is a Type 2 cystatin. The amino acid sequence is 73% identical with that of the cystatin in African-puff-adder (Bitis arietans) venom, with which it shares a unique six-residue insertion in a region opposite the reactive inhibitory site. Cobra cystatin is 25–42% identical with other Type 2 cystatins, the most closely related being the recently described human cystatin M, which also has a similar five-residue insertion starting at position 76 (chicken cystatin numbering). A molecular phylogenetic tree of 16 representative members of Family 2 cystatins was constructed by parsimony analysis; it suggests that snake cystatins, together with Tachypleus tridentatus (Japanese horseshoe crab) cystatin and human cystatin M, form a new subfamily within cystatin Family 2.

scholarly journals A novel cysteine proteinase inhibitor from seeds of Enterolobium contortisiliquum and its effect on Callosobruchus maculatus larvae

2021 ◽  
Vol 25 ◽  
pp. 100876
Author(s):  
Natalia N.S. Nunes ◽  
Rodrigo S. Ferreira ◽  
Leonardo F.R. de Sá ◽  
Antônia Elenir A. de Oliveira ◽  
Maria Luiza V. Oliva
Keyword(s):  
Proteinase Inhibitor ◽  
Callosobruchus Maculatus ◽  
Cysteine Proteinase ◽  
Cysteine Proteinase Inhibitor
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