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Genetic relationship between β-galactosidase and β-fucosidase in the mouse

✍ Scribed by Reza Seyedyazdani; Lars-G. Lundin

Book ID
104785121
Publisher
Springer
Year
1974
Tongue
English
Weight
384 KB
Volume
12
Category
Article
ISSN
0006-2928

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✦ Synopsis

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 a strong correlation between the activities of these two enzymes in different tissues ofF2 animals. A comparison of the fraetionation properties of fl-galactosidase and

[3-fucosidase showed that the two activities had a parallel distribution and identical thermostability. These data suggest that the same enzyme catalyzes the hydrolysis of both substrates.

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Relationship between genetic variation in thermal stability and electrophoretic mobility of mouse β-galactosidase
✍ Franklin G. Berger; Aldons J. Lusis 📂 Article 📅 1978 🏛 Springer 🌐 English ⚖ 376 KB

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