High impact information on OGCHI

• Three fractions were OMCHI variants differing in carbohydrate composition, especially in sialic acid content, and the other fraction was tentatively termed ovoglycoprotein (OGCHI) [1].
• However, neither the amino acid sequence of OGCHI nor the responsible part for the chiral recognition (protein domain or sugar moiety) has yet to be determined [2].
• It is suggested that the electrostatic interaction between an amino or carboxyl group of OGCHI and a charged solute should play an important role in chiral recognition of the solute [3].
• In the former case, OGCHI was bound to N,N'-disuccinimidyl carbonate-activated aminopropyl-silica gels, while in the latter case OGCHI activated by a water-soluble carbodiimide and N-hydroxysulfosuccinimide was bound to aminopropyl-silica gels [3].
• Separation of enantiomers on a chiral stationary phase based on ovoglycoprotein. II. Comparison of chiral recognition properties with crude ovomucoid [4].

Biological context of OGCHI

• These results reveal that the chiral recognition site(s) for OGCHI exists on the protein domain of OGCHI [5].

Associations of OGCHI with chemical compounds

• Resolution of dihydropyridine calcium antagonist enantiomers using HPLC with ovoglycoprotein as a chiral stationary phase [6].

Analytical, diagnostic and therapeutic context of OGCHI

• The isoelectric point (pI) of natural OGCHI was 4.37-4.51 by isoelectric focusing, while natural OGJPQ showed two discrete bands at pI 4.68 and 4.77 [7].
• The absence of chiral recognition ability in ovomucoid: ovoglycoprotein-bonded HPLC stationary phases for chiral recognition [1].
• Separation of enantiomers on a chiral stationary phase based on ovoglycoprotein. V. Influence of immobilization method on chiral resolution [3].

References