In:
Functional Plant Biology, CSIRO Publishing, Vol. 2, No. 1 ( 1975), p. 13-
Abstract:
The three globulins of the seeds of L. angustifolius cv. Uniwhite may be satisfactorily resolved in 10 min by electrophoresis on cellulose acetate strips. These globulins, conglutins α, β and γ, vary markedly in their amino acid compositions, with conglutin Ω differing from conglutins α and β and most other legume storage proteins in its relatively high content of cystine and methionine and lower content of arginine and glutamic acid.
When examined on sodium dodecyl sulphate-polyacrylamide gels, both in the absence and presence of β-mercaptoethanol, the three globulins were found to differ completely in the type of subunit proteins they contain and in the significance of intrachain disulphide bonding. Conglutin α was found to contain three or four types of non-covalently linked subunits with apparent molecular weights in the range 55 000-80 000, each of which may contain a disulphide-bonded moiety with a molecular weight near 20 000. Conglutin γ was found to contain disulphide-bonded chains of molecular weights 17 000 and 30 000, whereas the four major subunits of conglutin β, whose molecular weights lie in the range 20 000-60 000, were not covalently linked together. The latter globulin does not appear to be homogeneous, for it can be separated by fractional precipitation with ammonium sulphate into a series of fractions which differ markedly in the proportion of subunit types they contain.
Type of Medium:
Online Resource
ISSN:
1445-4408
Language:
English
Publisher:
CSIRO Publishing
Publication Date:
1975
SSG:
12
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