Autor: R A Kuhlmann, L M Likhosherstov, M D Martynova, I. Yu. Bakunina, Olga I. Nedashkovskaya, Valery V. Mikhailov, L A Elyakova
Rok vydání: 2002
Předmět:
Zdroj: Biochemistry (Moscow). 67:689-695
ISSN: 0006-2979
DOI: 10.1023/a:1016106623655
Popis: An alpha-N-acetylgalactosaminidase IV able to remove blood type specificity of human A(II)-erythrocytes and not effecting B(III)-erythrocytes was isolated from the marine bacterium Arenibacter latericius KMM 426T. The alpha-N-acetylgalactosaminidase IV preparation exhibits high activity during inhibition of hemagglutination with blood group substance A containing determinants analogous to A-erythrocytes. The enzyme has a pH optimum from 7.0 to 8.0 and completely retains its activity during 30-min heating at 50 degrees C and for a week at 20 degrees C. The enzyme can be stored under the sterile conditions for any length of time at 4 degrees C, but it does not withstand freezing. The alpha-N-acetylgalactosaminidase is resistant to NaCl; for p-nitrophenyl-alpha-N-acetyl-D-galactosaminide, the Km is 0.38 mM. The molecular mass of the enzyme determined by gel filtration is 84 kD.
Databáze: OpenAIRE