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. 1990 Oct;94(2):738–744. doi: 10.1104/pp.94.2.738

Partial Characterization and Subcellular Localization of Three α-Glucosidase Isoforms in Pea (Pisum sativum L.) Seedlings 1

Eric P Beers 1,2,3,2, Stanley H Duke 1,2,3, Cynthia A Henson 1,2,3
PMCID: PMC1077293  PMID: 16667773

Abstract

Three isoforms of α-glucosidase (EC 3.2.1.20) have been extracted from pea (Pisum sativum L.) seedlings and separated by DEAE-cellulose and CM-Sepharose chromatography. Two α-glucosidase isoforms (αG1 and αG2) were most active under acid conditions, and appeared to be apoplastic. A neutral form (αG3) was most active near pH 7, and was identified as a chloroplastic enzyme. Together, the activity of αG1 and αG2 in apoplastic preparations accounted for 21% of the total acid α-glucosidase activity recovered from pea stems. The vast majority (86%) of the apoplastic acid α-glucosidase activity was due to αG1. The apparent Km values for maltose of αG1 and αG2 were 0.3 and 1.3 millimolar, respectively. The apparent Km for maltose of αG3 was 33 millimolar. The respective native molecular weights of αG1, αG2, and αG3 were 125,000, 150,000, and 110,000.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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