Purification and characterization of moschins, arginine-glutamate-rich proteins with translation-inhibiting activity from brown pumpkin (Cucurbita moschata) seeds

T B Ng; A Parkash; W W Tso

doi:10.1016/s1046-5928(02)00500-4

Purification and characterization of moschins, arginine-glutamate-rich proteins with translation-inhibiting activity from brown pumpkin (Cucurbita moschata) seeds

Protein Expr Purif. 2002 Oct;26(1):9-13. doi: 10.1016/s1046-5928(02)00500-4.

Authors

T B Ng¹, A Parkash, W W Tso

Affiliation

¹ Department of Biochemistry, Faculty of Medicine, Basic Medical Sciences Bldg. Rm. 302B, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China. biochemistry@cuhk.edu.hk

PMID: 12356464
DOI: 10.1016/s1046-5928(02)00500-4

Abstract

From fresh brown pumpkin seeds, two proteins with a molecular mass of 12kDa and an N-terminal sequence rich in arginine and glutamate residues were obtained. The protein designated alpha-moschin closely resembled the fruitfly programmed-cell death gene product and the protein designated beta-moschin demonstrated striking similarity to prepro 2S albumin in N-terminal sequence. alpha- and beta-moschins inhibited translation in the rabbit reticulocyte lysate system with an IC(50) of 17 microM and 300nM, respectively.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Arginine / analysis*
Cucurbita / chemistry*
Electrophoresis, Polyacrylamide Gel
Glutamates / analysis*
Molecular Sequence Data
Plant Proteins / chemistry*
Plant Proteins / isolation & purification*
Plant Proteins / pharmacology
Protein Biosynthesis / drug effects*
Seeds / chemistry*
Sequence Homology, Amino Acid

Substances

Glutamates
Plant Proteins
Arginine