Suborganellar localization of proteinase catalyzing the limited hydrolysis of pumpkin globulin.

Abstract:

:Protein bodies were prepared from the cotyledons of pumpkin (Cucurbita sp.) seeds by employing a nonaqueous isolation method. Both light micrographic examination and the marker enzyme assays have shown that the isolated protein bodies were intact and contamination with other cell organelles or cytoplasmic components was negligible. A proteolytic enzyme catalyzing the limited hydrolysis of carboxymethylated gamma' chain of globulin was found to be present in the protein bodies. The specific activity in the protein body (18 units per milligram protein) was higher than that in the whole cell extract (13 units per milligram protein), indicating that the limited proteolytic enzyme was localized in the protein body.After lysis of the protein bodies using hypotonic buffer solution, the suborganellar components (matrix, membranes, and crystalloids) were separated by sucrose density gradient centrifugation. The crystalloid was composed of only globulin, a major seed protein. The major proteins of matrix and membrane fractions were shown to have mol wt of approximately 10,000. About 90% of the limited proteolytic activity was found in the matrix region.

journal_name

Plant Physiol

journal_title

Plant physiology

authors

Hara-Nishimura I,Nishimura M,Matsubara H,Akazawa T

doi

10.1104/pp.70.3.699

subject

Has Abstract

pub_date

1982-09-01 00:00:00

pages

699-703

issue

3

eissn

0032-0889

issn

1532-2548

journal_volume

70

pub_type

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