Untersuchungen an Rinderleberkatalase. II. Mitteil.: Die Aminosäuren des Proteins

Publisher Website
Google Scholar
Abstract
Needles of catalase were dried in vacuo and hydrolyzed with 5 [image] HC1 at 150[degree]C for 6 hours. The amino acids were separated by means of descending paper chromato-graphy using 4 solvent systems so that each amino acid was obtained well separated in at least one system. The following systems were used: Partridge mixture (n-butanol- water-acetic acid) for cystine, proline, tyrosine, valine + methionine; phenol saturated with borate buffer pH 12 for aspartic acid, glutamic acid, serine, glycine, threonine and alanine; o- cresol saturated with borate buffer pH 8.4 for valine and methionine; and pyridine: amyl alcohol: water 25:50:25 for leucine, isoleucine and phenyl alanine as well as for methionine and valine. Tryptophan was estimated in the unhydrolyzed protein with concentrated H2SO4 and p-dimethylaminobenzaldehyde. The amino acid spots on the chromatograms were treated with ninhydrin and copper nitrate, and the copper-ninhydrin complex extracted into methanol and measured at 470 m/i. The amino acid composition is given. It presents no unusual features.

This publication has 1 reference indexed in Scilit: