Genetic control of heat sensitivity and activity level of murine arylsulfatase B
โ Scribed by William L. Daniel
- Book ID
- 104784500
- Publisher
- Springer
- Year
- 1976
- Tongue
- English
- Weight
- 860 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0006-2928
No coin nor oath required. For personal study only.
โฆ Synopsis
BALB/c male mice possess twofold higher kidney p-nitrocatechol-SO4 arylsulfatase B than do A/HeJ male mice; however, their liver arylsulfatase activities are comparable. Twentyfold-purified kidney arylsulfatases B from these two strains have similar Michaelis constants, electrophoretic mobilities, pH optima, and inhibitor profiles; however, the BALB/c enzyme is more heat stable than the A/HeJ enzyme. BALB/c, C3H/HeJ, DBA/2J, and SWR/J mice share an autosomal allele, As-1a, which apparently determines the heat-stable arylsulfatase B, while A/HeJ and C57BL/6J mice possess the As-1b allele, which determines the heat-sensitive enzyme. A second autosomal locus, Asr-1, determines liver arylsulfatase B activity. C57BL/6J mice carry the Asr-1a allele, which results in high liver activities, while C3H/HeJ mice are homozygous for the low-activity allele, Asr-1b. Male mice generally have 30-40% higher kidney activities than females; however, female kidney arylsulfatase activities rise and actually surpass those of males during late pregnancy and lactation.
๐ SIMILAR VOLUMES
Two closely linked regulatory genes have been reported to control activity levels of beta-galactosidases in murine tissues. The specific effects of these genes on murine glycolipid metabolism have not been elucidated. A/HeJ kidney 4-methylumbelliferyl-beta-galactosidase exhibited lower thermostabili