The identification by sequence homology of stage-specific sea urchin embryo histones H1

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Abstract

The histone H1 fraction from gastrula of the sea urchin Parechinus angulosus consists of a mutitude of polypeptides with different electrophoretic mobilities. The synthesis of these proteins is programmed. Amino acid composition, electrophoretic properties and sequence homologies identify these as isohistones H1. One of these isohistones atypically binds the non-ionic detergent Triton X-100.

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    Data supplementary to this article are deposited with, and can be obtained from, Elsevier Science Publishers, B.V., BBA Data Deposition, P.O.Box 1345, 1000 BH Amsterdam, The Netherlands. Reference should be made to BBA/DD/265/31708/747(1983) 276. The supplementary information includes: the amino acid composition of P. angulosus embryo H1-1 and H1-2 and of the peptides produced by cyanogen bromide cleavage, and the quantitative evaluation of each sequencing cycle.

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