Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/98957
Type: Artigo de periódico
Title: Dimer-tetramer Transition In Hemoglobins From Liophis Miliaris-ii. Evidence With The Stripped Proteins
Author: Focesi Jr. A.
Ogo S.H.
Matsuura M.S.A.
Abstract: 1. 1. Whole Liophis miliaris hemolysate stored under refrigeration at pH 7 becomes progressively deoxygenated and presents two hemoglobin forms of mol. wts 32,500 and 64,000, consistent with oxydimers and deoxytetramers respectively. 2. 2. The Hill plot determined at pH 6.5 considering oxygen pressure capable to saturate up to 50% of the hemoglobin shows a coefficient value of nH = 2.06, whereas that found at higher oxygen pressure was nH = 0.85. 3. 3. The apparent Bohr effect of about ΔH+ = -0.4 in the stripped hemoglobin was explained by the increase of co-operative deoxytetramer T-state/non-co-operative ratio as a function of proton concentration. © 1990.
Editor: 
Rights: fechado
Identifier DOI: 10.1016/0305-0491(90)90351-S
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-0025236563&partnerID=40&md5=898a2cc84d3ce16c231d55e7f5fc3198
Date Issue: 1990
Appears in Collections:Unicamp - Artigos e Outros Documentos

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