Abstract
A single form of endopeptidase (EP-1) was found to be present at all stages of development and differentiation in all tissues of inbred maize. This endopeptidase occurs as two electrophoretically distinct variants which exist in different inbred maize lines. The gene coding for this endopeptidase has been tentatively located at or near the Y1 locus on chromosome 6. The EP-1 variants are under the control of two codominant alleles (Ep1A and Ep1B) at the Ep1 locus. The two endopeptidase variants are similar with respect to molecular weight, heat stability, Km, and metal ion inhibition, but are distinguishable by distinct isoelectric points as well as by different mobilities on starch gel electrophoresis. All attempts to hybridize the variants for purposes of determining subunit structure have failed. The endopeptidase is not inhibited by endogenous maize bovine trypsin inhibitor. During the development of seedlings, the endopeptidase is most active in immature liquid endosperm and in scutella, while the maize trypsin inhibitor is highest in starchy endosperm of mature kernels.
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