Proteolytic activity in anther extracts of fertile and cytoplasmic male sterile Petunia

Proteolytic activity is compared in anther extracts from Petunia parodii fertile and cytoplasmic male sterile lines. It is characterized relative to developmental stage of the anthers, effect of variable incubation times, pH of isolation buffers, and degradation of marker proteins. In fertile anther...

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Bibliographic Details
Published in:Plant physiology (Bethesda) 1985-09, Vol.79 (1), p.301-305
Main Authors: Wu, F.S, Murry, L.E
Format: Article
Language:English
Subjects:
Agronomy. Soil science and plant productions
ANTERA
ANTHERE
ANTHERS
Biological and medical sciences
Classical genetics, quantitative genetics, hybrids
ESTERILIDAD MASCULINA
Fertility
Fundamental and applied biological sciences. Psychology
Genetics and breeding of economic plants
Genetics of eukaryotes. Biological and molecular evolution
Heterosis. Floral biology applications: apomixy, male sterility, incompatibility, varia
Homogenization
INFERTILITE MALE
Male fertility
MALE INFERTILITY
Meiosis
Microsporogenesis
PETUNIA
petunia parodii
Plant breeding: fundamental aspects and methodology
PLANT EXTRACTS
Plant fertility
Plants
Pollen
PROTEOLISIS
PROTEOLYSE
PROTEOLYSIS
Pteridophyta, spermatophyta
Short Communications
Substrate specificity
Vegetals
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Summary:Proteolytic activity is compared in anther extracts from Petunia parodii fertile and cytoplasmic male sterile lines. It is characterized relative to developmental stage of the anthers, effect of variable incubation times, pH of isolation buffers, and degradation of marker proteins. In fertile anthers, proteolytic activity increases at the end of microsporogenesis and peaks early in microgametogenesis. Degradation is most severe in extracts of fertile anthers and in high molecular weight proteins and reaches its maximum within 20 minutes. Degradation of marker proteins is greatest at pH 5.6 to 8.0 in fertile anther extracts and is eliminated under strong acid conditions (pH 2.8 to 4.0) in both fertile and cytoplasmic male sterile anther extracts. Marker proteins degrade more severely in extracts of fertile anthers; however, the order of substrate sensitivity- myosin > phosphorylase b > bovine serum albumin and ovalbumin > β-galactosidase-is the same in extracts from fertile and cytoplasmic male sterile anthers.
ISSN:0032-0889
1532-2548
DOI:10.1104/pp.79.1.301