ALPHA-CHYMOTRYPSIN AS CATALYST FOR PEPTIDE-SYNTHESIS

[11] HESS GP, 1971, ENZYMES, V3, P213

[12] KIMMEL JR, 1957, ADV ENZYMOL, V19, P308

[13] AMINO ACID DERIVATIVES .2. ENZYMATIC SYNTHESIS OF PHENYLHYDRAZIDES OF CARBOALLYLOXYAMINO ACIDS [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1950, 72 (04) : 1742 - 1743

[14] ON SPECIFICITY OF BACILLUS SUBTILIS NEUTRAL PROTEASE IN RELATION TO COMPOUND ACTIVE SITE [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1969, 135 (1-2) : 311 - &

[15] COMPARATIVE SPECIFICITY OF MICROBIAL ACID PROTEINASES FOR SYNTHETIC PEPTIDES .3. RELATIONSHIP WITH THEIR TRYPSINOGEN ACTIVATING ABILITY [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1973, 157 (02) : 561 - 572

[16] COMPARATIVE STUDY OF VARIOUS SERINE ALKALINE PROTEINASES FROM MICROORGANISMS - ESTERASE-ACTIVITY AGAINST N-ACYLATED PEPTIDE ESTER SUBSTRATES [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1974, 165 (01) : 72 - 79

[17] COMPARISON OF ALPHA-CHYMOTRYPSIN AND SUBTILISIN BPN - SIZE AND SPECIFICITY OF ACTIVE SITE [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1969, 35 (02) : 210 - &

[18] KINETIC INVESTIGATION OF SUBSITES S-1' AND S-2' IN ALPHA-CHYMOTRYPSIN AND SUBTILISIN BPN' [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1977, 178 (01) : 188 - 194

[19] ON SIZE OF ACTIVE SITE IN PROTEASES .I. PAPAIN [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1967, 27 (02) : 157 - +

[20] THE PAPAIN-CATALYZED SYNTHESIS OF ACYL-D-PHENYLALANYLPHENYLHYDRAZIDES AND L-PHENYLALANYLPHENYLHYDRAZIDES FROM A SERIES OF ENANTIOMORPHIC PAIRS OF ACYLATED PHENYLALANINES [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1951, 73 (04) : 1644 - 1646

[11] HESS GP, 1971, ENZYMES, V3, P213

[12] KIMMEL JR, 1957, ADV ENZYMOL, V19, P308

[13] AMINO ACID DERIVATIVES .2. ENZYMATIC SYNTHESIS OF PHENYLHYDRAZIDES OF CARBOALLYLOXYAMINO ACIDS [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1950, 72 (04) : 1742 - 1743

[14] ON SPECIFICITY OF BACILLUS SUBTILIS NEUTRAL PROTEASE IN RELATION TO COMPOUND ACTIVE SITE [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1969, 135 (1-2) : 311 - &

[15] COMPARATIVE SPECIFICITY OF MICROBIAL ACID PROTEINASES FOR SYNTHETIC PEPTIDES .3. RELATIONSHIP WITH THEIR TRYPSINOGEN ACTIVATING ABILITY [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1973, 157 (02) : 561 - 572

[16] COMPARATIVE STUDY OF VARIOUS SERINE ALKALINE PROTEINASES FROM MICROORGANISMS - ESTERASE-ACTIVITY AGAINST N-ACYLATED PEPTIDE ESTER SUBSTRATES [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1974, 165 (01) : 72 - 79

[17] COMPARISON OF ALPHA-CHYMOTRYPSIN AND SUBTILISIN BPN - SIZE AND SPECIFICITY OF ACTIVE SITE [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1969, 35 (02) : 210 - &

[18] KINETIC INVESTIGATION OF SUBSITES S-1' AND S-2' IN ALPHA-CHYMOTRYPSIN AND SUBTILISIN BPN' [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1977, 178 (01) : 188 - 194

[19] ON SIZE OF ACTIVE SITE IN PROTEASES .I. PAPAIN [J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1967, 27 (02) : 157 - +

[20] THE PAPAIN-CATALYZED SYNTHESIS OF ACYL-D-PHENYLALANYLPHENYLHYDRAZIDES AND L-PHENYLALANYLPHENYLHYDRAZIDES FROM A SERIES OF ENANTIOMORPHIC PAIRS OF ACYLATED PHENYLALANINES [J]. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1951, 73 (04) : 1644 - 1646