| First Author | Daniel WL | Year | 1980 |
| Journal | Biochem Genet | Volume | 18 |
| Issue | 7-8 | Pages | 625-42 |
| PubMed ID | 7470017 | Mgi Jnum | J:6463 |
| Mgi Id | MGI:54939 | Doi | 10.1007/BF00484581 |
| Citation | Daniel WL, et al. (1980) Comparative biochemistry of murine arylsulfatase B. Biochem Genet 18(7-8):625-42 |
| abstractText | Arylsulfatase B was purified 4500-fold from liver and kidney of C57BL/6J mice. Hepatic and renal arysulfatase B are apparently determined by a single structural locus; however, posttranslational modification introduces inter- and intratissue microheterogeneity. Partially purified enzyme from C57BL/6J, A/J, C3H/HeJ, and SWR/J mice has similar catalytic properties. The 4500-fold-purified arylsulfatase B from SWR/J and C3H/HeJ mice was more thermostable than that from C57BL/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-1a allele (thermostable enzyme), while As-1b was largely restricted to A and C57 strains. |
