Amino Terminal Group in Chymotrypsinogen

Bovine Pancreatic Procarboxypeptidase B. II. Mechanism of Activation*

“…The aqueous phase of the hydrolysate contained neither di-DNP-histidine nor DNP-arginine. When the protein was denatured prior to dinitrophenylation, the hydrolysate contained an ether-soluble, brownish-yellow substance; this substance behaved on chromatography like the product reported by Bettelheim (1955) to arise during dinitrophenylation and hydrolysis of chymotrypsinogen A, which contains N-terminal half-cystine. Dinitrophenylation of performic acid-oxidized procarboxypeptidase B yielded 0.1 residue of DNP-cysteic acid per mole of protein and 0.07 residues of DNP-serine.…”

Mechanism of activation of trypsinogen and chymotrypsinogen

“…The protein is devoid of any reactive C-terminal groups 9 but contains one N-terminal half cystine. 20 Rapid activation of chymotrypsinogen (chymotrypsinogen, 40 m g / d ; trypsin, 1.2 mg/ml, sodium phosphate buffer pH 7.8,0.05 M, 0") is accompanied by changes in electrophoretic patterns and mobilities and by the appearance of terminal groups. Characteristic electrophoretic patterns obtained in the presence of DFP (acetate buffer pH 4.98, ionic strength 0.1) are shown in fig.…”

Terminal Amino Groups in Wool and S-Carboxymethyl Kerateine 2

“…of the wool yet contains the same N-terminal residues with the exception of valine. In view of the fact that no pure protein has given more than three different N-terminal residues, as in the case of a-chymotrypsin (Bettelheim 1955), while most have one or two terminal residues (Sanger 1955), it seems probable that the N-terminal residues observed in SCMK2 and wool are not stoichiometrically significant and represent slightly degraded cyclic molecules. For SCMK2, estimates of the molecular weight have been made in this Laboratory.…”