Acid-alkaline transition of a seaturtle myoglobin: coexistence at high ph of high and low spin forms (1985)
- Authors:
- USP affiliated authors: NASCIMENTO, OTACIRO RANGEL - IFSC ; TABAK, MARCEL - IQSC ; BAFFA FILHO, OSWALDO - FFCLRP
- Unidades: IFSC; IQSC; FFCLRP
- DOI: 10.1016/0167-4838(85)90174-8
- Subjects: BIOFÍSICA; SPIN
- Language: Português
- Source:
- Título: Biochimica Biophysica Acta
- Volume/Número/Paginação/Ano: v.832, p.62-8, 1985
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
-
ABNT
BAFFA, Oswaldo e TABAK, Marcel e NASCIMENTO, Otaciro Rangel. Acid-alkaline transition of a seaturtle myoglobin: coexistence at high ph of high and low spin forms. Biochimica Biophysica Acta, v. 832, p. 62-8, 1985Tradução . . Disponível em: https://doi.org/10.1016/0167-4838(85)90174-8. Acesso em: 22 fev. 2026. -
APA
Baffa, O., Tabak, M., & Nascimento, O. R. (1985). Acid-alkaline transition of a seaturtle myoglobin: coexistence at high ph of high and low spin forms. Biochimica Biophysica Acta, 832, 62-8. doi:10.1016/0167-4838(85)90174-8 -
NLM
Baffa O, Tabak M, Nascimento OR. Acid-alkaline transition of a seaturtle myoglobin: coexistence at high ph of high and low spin forms [Internet]. Biochimica Biophysica Acta. 1985 ;832 62-8.[citado 2026 fev. 22 ] Available from: https://doi.org/10.1016/0167-4838(85)90174-8 -
Vancouver
Baffa O, Tabak M, Nascimento OR. Acid-alkaline transition of a seaturtle myoglobin: coexistence at high ph of high and low spin forms [Internet]. Biochimica Biophysica Acta. 1985 ;832 62-8.[citado 2026 fev. 22 ] Available from: https://doi.org/10.1016/0167-4838(85)90174-8 - The acid alcaline transition and thermodenaturation of Aplysia brasiliana myoglobin
- The acid-alkaline transition of a sea turtle myoglobin
- On the interaction of small molecules with hemoglobin: orientational effects of hydration layers in protein crystal
- On the interaction of small molecules with hemoproteins: sperm whale myoglobin
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- Interaction of copper ions with turtle myoglobin
- Role distal histidine on the stabilization of the iron symmetry in hemoproteins: a electron paramagnetic resonance study
- Esr study of nitrosyl-aplysia brasiliana myoglobin and nitrosyl annelidae glossoscolex paulistus erythrocruorin
- Microenvironment of 'FE POT.3+' in aplysia brasiliana myoglobin: epr and optical absorption
- Interaction of aplysia brasiliana myogloblin with 'MN POT.2+' and 'CU POT.2+' ions
Informações sobre o DOI: 10.1016/0167-4838(85)90174-8 (Fonte: oaDOI API)
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