Plant Physiol.
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Plant Physiology 44:1488-1498 (1969)
© 1969 American Society of Plant Biologists

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Articles

Enzymes Associated with Protein Bodies Isolated from Ungerminated Barley Seeds

Robert L. Orya,1 and Knud W. Henningsenb

a Department of Biochemistry and Nutrition, Polytechnic Institute of Denmark, 2800 Lyngby, Institute of Genetics, University of Copenhagen, 1353 Copenhagen

Protein bodies were isolated intact from dormant barley seeds, Hordeum vulgare, var. Kenia, by a combination of buffer extractions and centrifugations over a sucrose gradient. Examination of the protein bodies pellet in the electron microscope shows 2 types of protein bodies in a wide variation of sizes. The majority of them stain evenly with osmium, are contained within a single membrane, and have no other structural components. The other type, mostly the larger particles, has a fine structure of orderly dark and light-stained layers attached to the protein bodies. Two acid hydrolases are associated with these particles: acid phosphatase activity, specific for sodium phytate but inactive on beta-glycerol phosphate, glucose 1-phosphate, fructose 1,6-diphosphate and adenosine triphosphate; and acid protease activity.

1 Fulbright-Hayes Research Scholar in Denmark, 1968-69. Permanent address: Southern Regional Research Laboratory, P.O. Box 19687, New Orleans, Louisiana. 70119 U.S.A. Requests for reprints should be sent to Prof. R. J. Djurtoft at the Polytechnic Institute.






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ASPB Publications PLANT PHYSIOLOGY THE PLANT CELL
Copyright © 1969 by the American Society of Plant Biologists