Please use this identifier to cite or link to this item:
|Type:||Artigo de periódico|
|Title:||Functional Properties Of Aplysia Brasiliana Myoglobin|
Focesi Jr. A.
|Abstract:||1. 1. The radular myoglobin of the Brazilian sea hare, Aplysia brasiliana, has been isolated and its ligand binding properties have been characterized. The myoglobin is similar to the myoglobin of Aplysia limacina (a Mediterranean species), and has a lower oxygen affinity than does myoglobin of the sperm whale, Physeter macrocephalus. 2. 2. Aplysia brasiliana myoglobin is a monomer and binds oxygen and other heme ligands non-cooperatively. There is no evidence of pH sensitivity in these processes. 3. 3. The kinetics of ligand binding and dissociation are simple processes. The lower oxygen affinity of Aplysia brasiliana myoglobin relative to sperm whale myoglobin is associated with a much higher rate of oxygen dissociation, with first order rate constants of 125 sec-1 and 10 sec-1 respectively. © 1978.|
|Appears in Collections:||Unicamp - Artigos e Outros Documentos|
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.