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Biochim Biophys Acta. 1993 Mar 5;1162(1-2):230-2.

Evidence from sequence analysis that hen egg-white ovomacroglobulin (ovostatin) is devoid of an internal beta-Cys-gamma-Glu thiol ester.

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  • 1Department of Molecular Biology, University of Arhus, Denmark.


53 residues of the internal sequence from the proteinase-binding hen egg-white ovostatin have been determined. The stretch corresponds to residues 945-997 of human alpha 2-macroglobulin. The degree of conservation of residues of the two stretches is approx. 74%. Cys-949, being one constituent of the internal thiol ester site of members of the family of proteins related to alpha 2-macroglobulin, is an Asn-residue in hen egg-white ovostatin, but the other constituent, Gln-952, is preserved. The Cys-to-Asn substitution forms the chemical basis for the lack of thiol esters in hen egg-white ovostatin.

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