𝔖 Bobbio Scriptorium
✦   LIBER   ✦

The genetics and biochemistry of urease inUstilago violacea

✍ Scribed by Michael L. Baird; Edward D. Garber

Publisher
Springer
Year
1981
Tongue
English
Weight
612 KB
Volume
19
Category
Article
ISSN
0006-2928

No coin nor oath required. For personal study only.

✦ Synopsis

Two complementing loci in different linkage groups of the basidiomycete Ustilago violacea are involved in urease activity: a structural one (ure-1) and a second inferred to involve a permease (ure-2) locus. Two types of complementing mutations occur in the structural locus: null activity (ure-l a) and obviously reduced activity (ure-l b). The ure-2 mutants lacked urease activity in vivo on the phenol red-urea test medium, but gave extracts with wild-type activity. Extracts from wild-type strains gave one site of urease activity after polyacrylamide gel electrophoresis. A number of ure-lb mutants and active revertants from ure-la mutants yielded electrophoretically variant urease sites. The results are discussed in terms of enzyme polymorphism in haploid eukaryotes by one (missense) or two (null then missense) mutations.

πŸ“œ SIMILAR VOLUMES

Developmental genetics of the soybean ur
Developmental genetics of the soybean urease isozymes
✍ Holland, Mark A. ;Griffin, Jeffrey D. ;Elise Meyer-Bothling, L. ;Polacco, Joseph πŸ“‚ Article πŸ“… 1987 πŸ› John Wiley and Sons 🌐 English βš– 863 KB

The soybean (Glycine max [L.] Merr.) contains two urease isozymes whose expression is regulated in a tissue-specific and temporal manner. The ubiquitous urease is expressed in all tissues examined (leaf, embryo, seed coat, cell culture); the embryo-specific urease is synthesized exclusively in the d

Genetics and biochemistry of the phenylk
Genetics and biochemistry of the phenylketonuria-present state
✍ K. BartholomΓ© πŸ“‚ Article πŸ“… 1979 πŸ› Springer 🌐 English βš– 290 KB

Phenylketonuria is an autosomal recessive inherited disease caused by a disturbance in the phenylalanine hydroxylating system. Phenylalanine is converted to tyrosine by phenylalanine hydroxylase, which is located mainly in the liver. This enzyme needs the reduced cofactor tetrahydrobiopterin to be a