A comparison of deacylation rates of para-substituted benzoyl-trypsins and chymotrypsins

Wang, Chih-Cheng; Shaw, Elliott

doi:10.1016/0003-9861(72)90034-3

Cited by 32 publications

(14 citation statements)

References 28 publications

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“…Bohak (Department of Biophysics, Weizmann Institute of Science, Rehovot, Israel). p-Nitrophenyl-p'-(co-dimethylsulphonioacetamido)benzoate bromide, a specific active-site titrant of chymotrypsin (Wang & Shaw, 1972), was a gift from Dr. E. Shaw. Diisopropyl phosphorofluoridate was purchased from Pierce Chemical Co. (Rockford, Ill., U.S.A.) and diluted with dry propan-2-ol.…”

Section: Methodsmentioning

confidence: 99%

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Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

Davidson

Gertler

Hofmann

1975

Biochemical Journal

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An acid proteinase from Aspergillus oryzae was isolated from a commercial powder by successive (NH4)2SO4 fractionation, acetone precipitation, and ion-exchange chromatography on phosphate- and DEAE-cellulose columns. The purified enzyme was found to be homogeneous by ultracentrifuge-sedimentation analysis (S20, W equal 3.63S), but electrofocusing in polyacrylamide gels and electrophoresis at pH 3.2 revealed that it consists of two very closely migrating bands. No difference in the amino acid composition and enzymic activities of the two partially separated bands could be detected, and it was concluded that the acid proteinase exists in two molecular forms. The enzyme activates bovine trypsinogen and chymotrypsinogen at pH 3.5 (the kappacat. and Km values at 35degrees C are 11.3S- minus 1, 0.10mM and 1.14S- minus 1, 0.18mM respectively). It hydrolyses the Phe-Phe bond of the synthetic pepsin substrates Z-His-Phe-Phe-OEt (kappacat. equal 1.65S- minus 1, Km equal 0.640mM at pH 3.5, 30degrees C) and Z-Ala-Ala-Phe-Phe-OPy4Pr (kappacat. equal 0.37S- minus 1, Km equal 0.037 mM at pH2.9, 39degrees C), where Z represents benzyloxycarbonyl and OPy4Pr represents 3-(4-pyridyl)-propyl 1-ester. Activation of bovine chymotrypsinogen results from the cleavage of the Arg(15)-Ile(16) bond in the zymogen. No other cleavages were observed. The use of A. oryzae proteinase provides a simple tool for the production of pi-chymotrypsin in good yield and purity.

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Section: Methodsmentioning

confidence: 99%

“…The spectrophotometric assay of chymotrypsin by using Bz-Tyr-OEt (0.0005M) was carried out at 25°C specific active-site titrant p-nitrophenyl-p'-(co-dimethylsulphonioacetamido)benzoate bromide (Wang & Shaw, 1972).…”

Section: Enzyme Assaysmentioning

confidence: 99%

Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

Davidson

Gertler

Hofmann

1975

Biochemical Journal

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“…In a previous study of the deacylation rates of a series of p-substituted benzoyl-trypsin and chymotrypsins (Wang and Shaw 1972), a good correlation was observed between k3 and the sigma values of the acyl groups. Plots of k3 versus sigma yielded slopes of 2 .…”

Section: Trans-isopropenylmentioning

confidence: 76%

Deacylation Rate Constants of Acylated Human and Porcine Plasmins

McLaren¹,

Tanizawa²

1984

Aust. Jnl. Of Bio. Sci.

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Deacylation rate constants, k3, were measured for the human acyl-plasmins which contain in the acyl portion, RCO, the R groups methyl, cyclohexyl, p-nitrophenyl, isobutyl, trans-isopropenyl, phenyl, a-naphthyl, anisoyl and p-guanidinophenyl. Values of k3 were also determined for the porcine acylplasm ins which have R = methyl, cyclohexyl, phenyl, anisoyl and p-guanidinophenyl. In general, for both the human and porcine acyl-plasm ins, k3 decreased as the electron-donating ability of the acyl group increased. At 25°C, the human acyl-plasmin with R = methyl has the highest k3, 1·06 ± 0·05 X 10-2 S-I, and the porcine acyl-plasmin with R = p-guanidinophenyl the lowest k3, 1·4 ± 0·1 X 10-6 S-I.

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“…Acetyl-L-alanyl-L-alanyl-L-alanine methyl ester (Ac-(Ala)s-OMe) and acetyl-L-tyrosine ethyl ester (Ac-Tyr-OEt) were purchased from Cyclo Chemical Co. p-Nitrophenyl-p'-(w-dimethylsulfonioacetamido)benzoate bromide, a specific activesite titrant of chymotrypsin (Wang and Shaw, 1972), was a gift of Dr. E. Shaw, and (V-rm-butyloxycarbonylglycyl-L-leucyl-L-phenylalanylchloromethane (Boc-Gly-Leu-Phe-CH2C1) was a gift of Dr. K. Kurachi. 4-Vinylpyridine was vacuum distilled before use.…”

Section: Methodsmentioning

confidence: 99%

Isolation and amino-terminal sequence analysis of two dissimilar pancreatic proelastases from the African lungfish, Protopterus aethiopicus

C¹,

Gertler²

1974

Biochemistry

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A comparison of deacylation rates of para-substituted benzoyl-trypsins and chymotrypsins

Cited by 32 publications

References 28 publications

Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

Aspergillus oryzae acid proteinase. Purification and properties, and formation of π-chymotrypsin

Deacylation Rate Constants of Acylated Human and Porcine Plasmins

Isolation and amino-terminal sequence analysis of two dissimilar pancreatic proelastases from the African lungfish, Protopterus aethiopicus

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