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. 1969 Nov;44(11):1488-1491, 1493, 1495, 1497-1498. doi: 10.1104/pp.44.11.1488

Enzymes Associated with Protein Bodies Isolated from Ungerminated Barley Seeds

Robert L Ory a,1, Knud W Henningsen b
PMCID: PMC396295  PMID: 5397495

Abstract

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 β-glycerol phosphate, glucose 1-phosphate, fructose 1,6-diphosphate and adenosine triphosphate; and acid protease activity.

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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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