Fluorescence studies of sds-hemoglobin of glossoscolex paulistus complexes: contribution to elucidation of protein structure (1997)
- Authors:
- Autor USP: TABAK, MARCEL - IQSC
- Unidade: IQSC
- Assunto: QUÍMICA ANALÍTICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquímica e Biologia Molecular
- Publisher place: São Paulo
- Date published: 1997
- Source:
- Título: Programa e Resumos
- Conference titles: Reunião Anual da Sbbq
-
ABNT
GELAMO, E L e TABAK, Marcel. Fluorescence studies of sds-hemoglobin of glossoscolex paulistus complexes: contribution to elucidation of protein structure. 1997, Anais.. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular, 1997. . Acesso em: 27 dez. 2025. -
APA
Gelamo, E. L., & Tabak, M. (1997). Fluorescence studies of sds-hemoglobin of glossoscolex paulistus complexes: contribution to elucidation of protein structure. In Programa e Resumos. São Paulo: Sociedade Brasileira de Bioquímica e Biologia Molecular. -
NLM
Gelamo EL, Tabak M. Fluorescence studies of sds-hemoglobin of glossoscolex paulistus complexes: contribution to elucidation of protein structure. Programa e Resumos. 1997 ;[citado 2025 dez. 27 ] -
Vancouver
Gelamo EL, Tabak M. Fluorescence studies of sds-hemoglobin of glossoscolex paulistus complexes: contribution to elucidation of protein structure. Programa e Resumos. 1997 ;[citado 2025 dez. 27 ] - Estudos cinéticos da influência de surfactantes iônicos na hemoglobina extracelular de Glossoscolex paulistus em meio ácido
- Protein concentration effect on thermal stability of the extracellular hemoglobin of glossoscolex paulistus: dynamic light scaterring and differential scanning calorimetry
- Spin-lattice relaxation in the 'GAMA IND.8'('Dy IND.3+':Ca'F IND.2','Nd IND.3+':Ca'F IND.2') quadruplets
- Dipyridamole interacts with the polar part of cationic reversed micelles in chloroform: 'ANTPOT.1 H' NMR and ESR evidence
- Stable nitroxyl radicals and dipyridamole in its ground and 'S IND.1'excited states form metastable complexes
- Different micellar packing and hydrophobicity of the membrane probes TEMPO and TEMPOL influence their partition between aqueous and micellar phases rather than location in the micelle interior
- Antioxidant effect of dipyridamole and its derivative RA-25 in mitochondria: correlation of activity and location in the membrane
- Dipyridamole effect on the electron transport kinetics in reaction centers from purple photosynthetic bacteria rhodobacter sphaeroides
- Interaction of dipyridamole with anionic phospholipid vesicles: fluorescence studies
- Antioxidant effect of dipyridamole (DIP) and its derivative RA 25 upon lipid peroxidation and hemolysis in red blood cells
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