Comparative biochemistry of murine arylsulfatase B

✍ Scribed by William L. Daniel; Michael S. Caplan

• Book ID: 104784090
• Publisher: Springer
• Year: 1980
• Tongue: English
• Weight: 827 KB
• Volume: 18
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00484581

✦ Synopsis

6J and A/J mice, strongly suggesting that the thermostability difference reflects an alteration of the primary structure of the enzyme. Thermal stability of arylsulfatase B was pH dependent and markedly influenced by buffer anion. Variation of thermostability did not appear accountable for the observed activity variation among these strains; however, this possibility cannot be rigorously excluded by presently available data. Thirty-five murine strains were found to possess the As-1 a allele (thermostable enzyme), while As-1 b was largely restricted to A and C57 strains.