Herbert Hanson

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Since it was shown in a previous report (1) that certain peptidases were capable of hydrolyzing peptides containing @alanine, the present investigation was undertaken to determine the possible metabolic fate of the naturally occurring peptide, carnosine. Although this substance, /3-alanyl-Lhistidine, has long been known and is one of the most abundant of(More)
1. Cathepsin H is an endoaminopeptidase belonging to the group of thiol enzymes. It was purified from rat liver lysosomes by gel filtration on Sephadex G-75, chromatography on CM-Sephadex C-50, on DEAE-Cellulose DE-52 and subsequently on an organomercurial absorbent. 2. The molecular weight of cathepsin H was found to be 28,000 and the isoelectric point was(More)
The construction of a simple and effective sample stirring device for commercial spectrophotometers and its use for continuous kinetic measurements and active site titrations with immobilized enzymes is described. Sepharose-bound leucine aminopeptidase and trypsin were selected as model enzymes to test the performance of the magnetic stirring equipment.(More)