Linked Life Data

3242545

Source:http://linkedlifedata.com/resource/pubmed/id/3242545

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
1989-5-30
pubmed:abstractText
The primary structures of alpha I- and beta I-chains from the hemoglobins of the Common Iguana (Iguana iguana) are presented. The globin chains were separated on CM-cellulose in 8 M urea buffer. The amino-acid sequences were established by automatic Edman degradation of the native chains, the tryptic peptides and a peptide obtained by cyanogen bromide cleavage. The sequences are compared with human hemoglobin. Amino-acid replacements at positions critical for structure and function of the hemoglobin are discussed. The requirements for binding of ATP and also of DPG as allosteric effectors at the beta-chains seem to be fulfilled. Comparison of the alpha-chains with those of the Viper (Vipera aspis) shows 66 amino-acid substitutions. This number is in the same order of magnitude as the ones found by comparison with alpha-chains of crocodiles and mammals as well as with alpha A-chains of a turtle and birds. This result points towards a period of independent evolution of the reptile lines leading to the Common Iguana on one hand and to the Viper on the other. This time span is comparable to the one separating mammals from reptiles.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0177-3593
pubmed:author
pubmed:issnType
Print
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1143-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Hemoglobins of reptiles. The primary structures of the alpha I- and beta I-chains of common iguana (Iguana iguana) hemoglobin.
pubmed:affiliation
Max-Planck Institut für Biochemie, Abteilung Proteinchemie, Martinsried bei München.
pubmed:publicationType
Journal Article, Comparative Study