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1
Studies on enzymatically active fragments of pepsin. III. Further purification and the homogeneity of a fragment with peptic activity.
J Biochem. 1962 Aug;52:103-7. doi: 10.1093/oxfordjournals.jbchem.a127577.
2
Studies on enzymatically active fragments of pepsin. II. Isolation and purification of fragments with peptic activity.
J Biochem. 1961 Apr;49:297-302. doi: 10.1093/oxfordjournals.jbchem.a127298.
3
[On the peptic and catheptic activity of pepsin preparations. Part 2].
Dtsch Gesundheitsw. 1959 Oct 22;14:1989-94.
4
A pepsin preparation without transpeptidation activity.
Biochim Biophys Acta. 1960 Jul 1;41:370-1. doi: 10.1016/0006-3002(60)90030-5.
5
The chromatographic purification of pepsinogen.
Biochim Biophys Acta. 1960 Jan 29;37:522-4. doi: 10.1016/0006-3002(60)90510-2.
6
[On the decomposition of beta-casein by pepsin].
Biochem Z. 1960;332:307-14.
7
Studies of the intermediates produced during peptic digestion of bovine serum albumin, ribonuclease and trypsin.
Arch Biochem Biophys. 1961 Jan;92:58-68. doi: 10.1016/0003-9861(61)90218-1.
8
The effect of sodium chloride on peptic digestion of bovine serum albumin.
Biochim Biophys Acta. 1961 Jan 15;46:381-3. doi: 10.1016/0006-3002(61)90762-4.
9
The denaturation of pepsin. IV. The effects of temperature.
Biochim Biophys Acta. 1960 Feb 12;38:113-22. doi: 10.1016/0006-3002(60)91200-2.
10
[Further investigations on the low-molecular products of the splitting of hemoglobin by pepsin].
Vopr Med Khim. 1959 Jul-Aug;5:265-73.
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