Purification and Characterization of a Cysteine Proteinase Inhibitor(Cystatin) from Seeds of Foxtail Millet, Setaria italica.
|
Accession number;00A0301130
|
| Title;Purification and Characterization of a Cysteine Proteinase Inhibitor(Cystatin) from Seeds of Foxtail Millet, Setaria italica. |
| Author;
TASHIRO MISAO
(Mukogawa Women's Univ., Fac. of Human Environmental Sci.)
KURATA AKIE
(Koka Women's Jr. Coll.)
HASEGAWA ATSUKO
(Otsuka Foods Co., Ltd.)
SAWADA SAYURI
(Mukogawa Women's Univ., Fac. of Human Environmental Sci.)
|
Journal Title;Journal of the Japanese Society for Food Science and Technology
|
Journal Code:F0895A
|
ISSN:1341-027X
|
|
VOL.47;NO.2;PAGE.105-111(2000)
|
| Figure&Table&Reference;FIG.7, TBL.2, REF.20 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;A cysteine proteinase inhibitor was purified from the extract of seeds of foxtail millet, Setaria italica, to an electrophoretically homogeneous protein by heat treatment, salting-out, ion-exchange chromatography on DEAE-Sepharose CL-6B, gel filtration on Sephadex G-50, and chromatofocusing on PBE 94. The inhibitor(FMCPI) was a single polypeptide with a molecular weight of 12000 and an isoelectric point of 5.2. It possessed the amino acid composition characterized by fairly high contents of aspartic acid, glutamic acid, and alanine and by no half-cystine. FMCPI was relatively thermostable since it maintained more than 50% of the original activity after treatment of 100.DEG.C. for 20min at pH2 or 7. However, the inhibitor almost lost its whole activity by the above treatment at pH10. FMCPI inhibited papain in a 1:1 protein molar ratio: the Ki value was 2.4*10-11M. Complex formation between FMCPI and papain derivatives demonstrated that the inhibitor was capable of combining with even a papain molecule without the catalytic ability. (author abst.) |
|
|
|
Related Articles;
|
|
