Purification and characterization of two basic spermatid-specific proteins isolated from the dog-fish Scylliorhinus caniculus.

Abstract:

:In dog-fish spermatid nuclei two intermediate proteins S1 and S2 replace histones before the setting down of protamines. These spermatid-specific proteins were isolated by carboxymethyl-cellulose chromatography and purified by high pressure liquid chromatography. S1 and S2 are characterized by a high content of basic residues and by the lack of cysteine and phenylalanine. The determination of their amino acid composition and of their N- and C-terminal sequences prove that each protein corresponds to a specific molecule which can be considered neither as a histone hydrolytic product nor as a protamines precursor.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Chauviere M,Laine B,Sautiere P,Chevaillier P

doi

10.1016/0014-5793(83)80386-x

subject

Has Abstract

pub_date

1983-02-21 00:00:00

pages

231-5

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(83)80386-X

journal_volume

152

pub_type

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