## Evidence for the identity of fl-galactosidase and fl-fucosidase enzymes in the house mouse was obtained by examination of the enzyme activities in animals from different crosses between C57BL/Kl mice with high galaetosidase and fucosidase activities and DBA/2/Kl mice with low activities. There is
Relationship between genetic variation in thermal stability and electrophoretic mobility of mouse β-galactosidase
✍ Scribed by Franklin G. Berger; Aldons J. Lusis
- Book ID
- 104783690
- Publisher
- Springer
- Year
- 1978
- Tongue
- English
- Weight
- 376 KB
- Volume
- 16
- Category
- Article
- ISSN
- 0006-2928
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✦ Synopsis
We have examined the relationships between the genetic determinants for mouse beta-galactosidase heat stability and electrophoretic mobility, in order to clarify previous reports indicating that a variation for enzyme heat stability is restricted to kidney while that for electrophoretic mobility is expressed in all tissues. We find that the two phenotypes show concordant strain distributions and cosegregate in genetic crosses. In contrast to a previous report, the thermal stability variation is expressed in all tissues, although the absolute rate of enzyme inactivation is tissue specific. The evidence supports the notion that a single beta-galactosidase structural locus is expressed in all tissues and that the differences in enzyme stability between tissues results from posttranslational enzyme modification.
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