Studies on castor bean hemagglutinin. III. Reinvestigation of the purification and characterization of castor bean hemagglutinin.
نویسندگان
چکیده
منابع مشابه
Purification of pyruvate kinase from germinating castor bean endosperm.
Cytosolic pyruvate kinase from endosperm of germinating castor beans (Ricinus communis L.; cv Hale) has been purified 3100-fold to apparent homogeneity and a final specific activity of 203 micromole pyruvate produced/minute per milligram protein. Purification steps included: heat treatment, polyethylene glycol fractionation, Q-Sepharose, ADP-agarose, Mono-Q and Phenyl Superose chromatography. N...
متن کاملLectins in castor bean seedlings.
The amounts of the two lectins (ricin and Ricinus communis agglutinin) in tissues of castor bean seedlings were followed during germination and early growth. For measurement, lectins in extracts were separately eluted from Sepharose columns; an antibody to the agglutinin was also used to detect the lectins by immunodiffusion. The endosperm of the dry seed contains 3.5 mg total lectin (5.6% of t...
متن کاملChemical modification studies on Ricinus communis (Castor Bean) agglutinin.
Ricinus communis agglutinin was subjected to various chemical treatments and the effect on its hemagglutinating and saccharide-binding properties was studied. Acetylation, succinylation and citraconylation led to a complete loss in the activity of the agglutinin, whereas reductive methylation had no effect on the activity, showing that charged amino groups were involved in the hemagglutinating ...
متن کاملProteases and Peptidases of Castor Bean Endosperm
The endosperm of castor bean seeds (Rkinus comunuis L.) contains two -SH-dependent amptidases, one hydrolyzing L-leucine-,Bnaphthylamide optimally at pH 7.0, and the other hydrolyzing L-proline,B-naphthylamide optimally at pH 7.5. After germination the endosprm contains in addition an -SH-dependent hemoglobin protease, a serinedependent carboxypeptidase, and at least two -SH-dependent enzymes h...
متن کاملEvidence that the castor bean allergens are the albumin storage proteins in the protein bodies of castor bean.
The well characterized castor bean (Ricinus communis L.) allergens were identified as the low molecular weight albumin storage proteins in the matrix of the protein bodies in the endosperm. The methods of identification involved molecular weight estimation, amino acid composition, stability at 100 degrees C, solubility in various solvents, gel electrophoresis, and immunological techniques. The ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1977
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.41.1069