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The Sp 1 Locus in Soybean Codes for β‐amylase 1
Author(s) -
Hildebrand D. F.,
Hymowitz T.
Publication year - 1980
Publication title -
crop science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.76
H-Index - 147
eISSN - 1435-0653
pISSN - 0011-183X
DOI - 10.2135/cropsci1980.0011183x002000020004x
Subject(s) - amylase , biology , locus (genetics) , starch , amylopectin , glycine , hydrolysis , alpha amylase , genotype , enzyme , gene , biochemistry , amylose , amino acid
One hundred F 2 soybean [ Glycine max (L.) Merrill] seeds from the cross PI 87525 ✕ ‘Ebony’ and 116 cultivars from Maturity Groups 00 through IV were analyzed using polyacrylamide gel electrophoresis and amylase assays to determine whether Sp 1 a and Sp 1 b seed protein bands were the same as the slow and fast amylase variant bands. In the PI 87525 ✕ Ebony cross, the slow and fast amylase variant bands had precisely the same segregation ratios and the same electrophoretic mobilities as the Sp 1 a and Sp 1 b protein bands. For 114 out of 116 cultivars tested, exact correspondence was obtained for Sp 1 a and slow amylase bands, and Sp 1 b and fast amylase bands. ‘Chestnut’ lacked an amylase band, however, the Sp 1 a seed protein band was present. ‘Altona’ was a mixture of genotypes that lacked or had the amylase band. The Altona genotype that had the fast amylase band also had the Sp 1 b band. The Altona genotype that lacked an amylase band also lacked a Sp 1 seed protein band. From the data obtained, we believe that the slow and fast amylase bands are the Sp 1 a and Sp 1 b seed protein bands. The use of selective α and β‐amylase inhibition and studies of the hydrolysis of amylopectin by the amylase variant support the hypothesis that the Sp 1 locus in soybeans codes for β‐amylase.