¹ From the Department of Biochemistry, College of Physicians and Surgeons, Columbia University, New York

1. A preparation of chymotrypsinogen, obtained from Dr. M. Kunitz, was analyzed for sulfur, the sulfur amino acids, tyrosine, and tryptophane.

2. The protein sulfur of chymotrypsinogen was accounted for as methionine, cysteine, and cystine.

3. A method is presented for calculating the minimum molecular weight of a protein from the distribution of the sulfur amino acids. In the case of chymotrypsinogen, the calculated minimum molecular weight was found to be the actual molecular weight.

4. The molecular weight of chymotrypsinogen is 36,700 by amino acid analysis as compared to 36,000 by osmotic pressure measurements of Kunitz and Northrop. Chymotrypsinogen contains per mol 17 atoms of sulfur, 3 residues of methionine, 4 of cysteine, 10 of half-cystine (i.e. 5 S—S linkages), 6 of tyrosine, and 10 of tryptophane.

5. The tryptophane content of chymotrypsinogen (5.51 per cent) is the highest of any protein so far on record.

6. Chymotrypsinogen contains no reactive SH groups, although it yields cysteine on hydrolysis. This may be due either to preformed but unreactive SH groups or to S—X groups. The term S—X group is used to denote the substitution of the sulfhydryl hydrogen by a constituent X; hydrolysis yields SH groups: S—X + HOH = SH + X—OH.

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