Linked Life Data

2258402

Source:http://linkedlifedata.com/resource/pubmed/id/2258402

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1991-1-31
pubmed:abstractText
Immobilized metal affinity chromatography was investigated for the fractionation of basic nuclear proteins of human sperm. Human sperm nuclei essentially contain two classes of protamines: a protamine of type P1 (HPl), rich in cysteine but with only one histidine, and three protamines of type P2 (HP2, HP3, HP4), rich in cysteine and histidine (nine in protamine HP2), potential ligands for transition metal ions. The critical conditions for metal affinity chromatography were defined: choice of metal, protein material and buffer, type of elution and sample loading. Chromatography of nuclear proteins, without histones and with cysteine residues alkylated by iodoacetamide, was optimum on zinc Chelating Sepharose in a Tris-acetate buffer and elution with an increasing concentration gradient of imidazole. Under these conditions, the two classes of protamines were completely separated. The intermediate basic proteins were further purified by reversed-phase high-performance liquid chromatography. Heterogeneity of binding to zinc of protamine HP1 was demonstrated. The proposed method is simple and reproducible and the recovery of proteins is high. It may be applied to study the expression and function of P1 and P2 protamines, e.g., in the case of infertile men.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9673
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
518
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Fractionation of basic nuclear proteins of human sperm by zinc chelate affinity chromatography.
pubmed:affiliation
URA CNRS 409, Institut de Recherches sur le Cancer de Lille, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't