Comparison of Protein Constituents Relating to beta-Glucosidase Activity in BB and bb Inbred Lines of MELILOTUS ALBA.

نویسندگان

  • D G Gilchrist
  • F A Haskins
  • H J Gorz
چکیده

I N biennial white-blossomed sweetclover (Melilotus alba Desr.) , the B/b allelic pair controls .&glucosidase activity ( SCHAEFFER, HASKINS and GORZ 1960; HASKINS and GORZ 1965). Homogenates of BB and Bb plants are high and iatermediate, respectively, in /3-glucosidase activity. No activity has been detected in homogenates of bb plants. The precise effect of the alleles B and b on the enzyme has not been investigated beyond the determination that lack of activity in bb homogenates is not due to soluble ,&glucosidase inhibitors (SCHAEFFER, HASKINS and GORZ 1960). Products of mutant alleles in the form of catalytically inactive but serologically cross-reacting proteins have been demonstrated in microbial systems. For example, among the tryptophan synthetase-deficient mutants of Neurospora crassa (SUSKIND, YANOFSKY and BONNER 1955) and Escherichia coli (LERNER and YANOFSKY 1957), certain mutants produce proteins which, though catalytically different, are sufficiently similar to Eormal tryptophan synthetase to be recognized by anti-tryptophan synthetase antibodies. In view of the results obtained in these and other studies employing microbial enzyme systems, experiments were undertaken to determine whether sweetclover plants of the bb genotype form a catalytically inactive protein which is closely related to p-glucosidase. These studies are the subject of this report.

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عنوان ژورنال:
  • Genetics

دوره 66 2  شماره 

صفحات  -

تاریخ انتشار 1970