Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles (1994)
- Authors:
- Autor USP: GURALNIK, HERNAN CHAIMOVICH - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Language: Inglês
- Imprenta:
- Publisher: Sociedade Brasileira de Bioquimica e Biologia Molecular
- Publisher place: São Paulo
- Date published: 1994
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reuniao Anual da Sociedade Brasileira de Bioquimica e Biologia Molecular
-
ABNT
VALENTE, A P C; ALMEIDA, F C L; CHAIMOVICH GURALNIK, Hernan. Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles. Anais.. São Paulo: Sociedade Brasileira de Bioquimica e Biologia Molecular, 1994. -
APA
Valente, A. P. C., Almeida, F. C. L., & Chaimovich Guralnik, H. (1994). Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles. In Programa e Resumos. São Paulo: Sociedade Brasileira de Bioquimica e Biologia Molecular. -
NLM
Valente APC, Almeida FCL, Chaimovich Guralnik H. Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles. Programa e Resumos. 1994 ; -
Vancouver
Valente APC, Almeida FCL, Chaimovich Guralnik H. Effect of the treatment with neuraminidase the behavior of alkaline phosphatase in micelles. Programa e Resumos. 1994 ; - Peg changes the fusion pattern in the case of unmodified fusogenic peptides
- Micelar and vesicular effects on reaction mechanisms
- `Beta´-2-glycoprotein I induces leakage from cardioliopin-containing vesicles by a non-fusion mechanism: binding, bilayer unsteady, aggregation and leakage
- Sera from patients with chronic chagas' disease may exhibit anti-cardiolipin activity
- Entrevista com o Prof. Hernan Chaimovich
- Autonomia?
- Pesquisa a serviço do desenvolvimento
- Prefácio da 1ª edição
- Estrutura e reatividade em micelas
- Stability and activity modulation of chymotrypsin in AOT reserved micelles by protein-interface interaction of ALPHA-chymotrypsin with a negative interface leads to cooperative breakage of a salt bridge that keeps the catalytic active conformation [ILe (16) - Asp(194)]
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