
TY  - JOUR
A1  - Blagrove, RJ 
A1  - Gillespie, JM 
T1  - Isolation, Purification and Characterization of the Seed Globulins of <I>Lupinus angustifolius</I>
JF  - Functional Plant Biology
JO  - Functional Plant Biol.
Y1  - 1975
VL  - 2
IS  - 1
SP  - 13
EP  - 27
KW  - 
UR  - https://doi.org/10.1071/PP9750013 
N2  - 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 &#945;, &#946; and &#947;, vary markedly in their amino acid compositions, with conglutin &#937; differing from conglutins &#945; and &#946; 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 &#946;-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 &#945; 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 &#947; was found to contain disulphide-bonded chains of molecular weights 17 000 and 30 000, whereas the four major subunits of conglutin &#946;, 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. 
ER  -

