Hydrogen ion titration behaviour of protein carmin from safflower seed (Carthamus tinctorius L.)

Prakash, V. and Latha, T. S. (1986) Hydrogen ion titration behaviour of protein carmin from safflower seed (Carthamus tinctorius L.). Acta Alimentaria, 15 (4). 281-289, 11 ref..

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Abstract

Studies on the dissociation and denaturation of carmin (mol. wt. approx. 260 000), a protein isolated from safflower seed, indicate that the binding of protons is of considerable importance in the stability of the quaternary structure of carmin. In the present work, carmin was examined by potentiometric titration in 0.5 M KCl over the full pH range; or by spectrophotometric titration by adjusting the pH of the protein solution with NaOH and measuring the absorbance at 295 nm. Results indicated that carmin has normal pKint values for the side chain carboxyl, imidazole and epsilon-amino groups. Tyrosyl phenol groups, however, showed an abnormal value of pKint of 10.75. Such findings indicate that most of the charged groups are available on the surface of the protein, whereas hydrophobic tyrosyl groups are embedded more deeply in the protein.

Item Type:	Article
Uncontrolled Keywords:	DENATURATION-; safflower seeds carmin, dissociation-denaturation & properties of; OILSEEDS-; safflower seeds carmin, protons binding & stability of; BINDING-; STABILITY-
Subjects:	500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry 600 Technology > 08 Food technology > 19 Lipids-oils/fats > 01 Oilseeds
Divisions:	Protein Chemistry and Technology
Depositing User:	Food Sci. & Technol. Information Services
Date Deposited:	18 Aug 2021 11:16
Last Modified:	18 Aug 2021 11:16
URI:	http://ir.cftri.res.in/id/eprint/6447

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