On the size of the active site in proteases. I. Papain.

Acetylornithinase of Escherichia coli: partial purification and some properties.

The preparation and properties of two new chromogenic substrates of trypsin.

https://www.farm.ucl.ac.be/Full-texts-FARM/Danhier-2010-2.pdf

To exploit the tumor microenvironment: Passive and active tumor targeting of nanocarriers for anti-cancer drug delivery

The spectrophotometric procedure proposed by Schwert and Takenaka for the assay of chymotrypsin and trypsin has been modified and extended to include the application to N-benzoyl-L-tyrosine ethyl e...

A modified spectrophotometric determination of chymotrypsin, trypsin, and thrombin.

An Aminoacyltransferase Preparation from Beef Liver

Regarding the general nature of catheptic enzymes.

The Specificity of Proteinases

apparently had some qualms) there can be disagreement; since further experience will doubtless settle these questions, there is no point discussing any of them here. The text is divided into twenty chapters, grouped in three units, on nutrition, metabolism, and growth and development. The first unit treats photosynthesis, mineral and water relations, and translocation. The second part includes chapters on enzymes, carbohydrates, respiration, and other metabolic processes and substances. This is essentially a brief treatment of plant biochemistry, assuming on the student's, part a knowledge of elementary chemistry and botany. The last unit, on growth and development, includes lengthy discussions of growth substances and the physiology of reproduction and differentiation. There is also a short section, \"Plant and Environment,\" on the autecological aspects of physiology.

Modern Trends in Physiology and Biochemistry.

The rates of the pepsin-catalyzed synthesis of oligopeptides of the general type A-Phe-Leu-B by the condensation of A-Phe-OH with H-Leu-B have been determined by means of analytical high performance liquid chromatography. Variation of the A group led to large changes in the initial rates of the condensation reaction, and the effect of such changes was found to be similar to that previously found for the secondary specificity of pepsin in the hydrolysis of oligopeptide substrates. Replacement of the Phe and Leu residues of A-Phe-OH or H-Leu-B by other amino acid residues gave relative rates of synthesis in accord with the known primary specificity of the hydrolytic action of pepsin. Partially-acetylated pepsin, which exhibits enhanced hydrolytic activity, also catalyzed the condensation reaction more effectively. The results are discussed in relation to the potential utility and limitations of pepsin as a catalyst in the preparative synthesis of oligopeptides and to the problem of the mechanism of its action.

Joseph S. Fruton

Papers

An Aminoacyltransferase Preparation from Beef Liver

Regarding the general nature of catheptic enzymes.

The Specificity of Proteinases

Modern Trends in Physiology and Biochemistry.

Specificity of pepsin-catalyzed peptide bond synthesis.