Über fermentative Desaminierung im Muskel.

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Abstract
Rabbit muscle contains enzymes capable of deaminizing ade-nosin or adenylic acid but not able to attack adenine in the form of the free purin base. Guanine, guanosin, and guanosinphosphoric acid from yeast nucleic acid were not attacked by the muscle enzymes. Ammonia formation from adenosin and from adenylic acid are produced by two ferments, one of which attacks only adenosin and the other only adenylic acid. The latter can be separated from the former by adsorbing it on aluminum hydroxide and eluting with sodium phosphate. The enzyme which splits adenosin remains in the extract, not being adsorbed. The pH range at which deaminiza-tion will take place is from about 4.5-9.2; the optimum lies in the narrow range of 5.7-6.15. The adenylic acid deaminase showed a high grade of specificity since it did not produce ammonia from glycocoll, d,l-alanine, 1-cys-tine, d,i-serine, d.l-phenylalanine, 1-tyrosine, 1-trypto-phane, 1-histidine, d,l-leucine, d,l-isoleucine, d,l-nor-leucine, d-glutamic acid, ghitamine, d,l-alanylglycine, d,l-leucylglycine, taurinc, creatine. creatinin. urea, guani-dine, or the purine bases. The adenylic acid from yeast is not attacked by the deaminizing enzyme from muscle. It is therefore apparently an isomere of the muscle compound. In addition to the deaminases which can produce ammonia from the adenine compounds there is a deaminase, which can form inosinic acid from muscle adenylic acid.

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