Biochemical and immunological characterization of acid phosphatases from n. Crassa (1991)
- Authors:
- USP affiliated authors: ROSSI FILHO, ANTONIO - FFCLRP ; BARBOSA, JOSE ELPIDIO - FMRP
- Unidades: FFCLRP; FMRP
- Subjects: IMUNOLOGIA; MICROBIOLOGIA; PARASITOLOGIA
- Language: Inglês
- Imprenta:
- Source:
- Título: Resumos
- Conference titles: Reunião Anual da Sbbq
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ABNT
HAN, S W et al. Biochemical and immunological characterization of acid phosphatases from n. Crassa. 1991, Anais.. Caxambú: Sbq, 1991. . Acesso em: 30 dez. 2025. -
APA
Han, S. W., Barbosa, J. E., Rossi, A., & Michelin, M. A. (1991). Biochemical and immunological characterization of acid phosphatases from n. Crassa. In Resumos. Caxambú: Sbq. -
NLM
Han SW, Barbosa JE, Rossi A, Michelin MA. Biochemical and immunological characterization of acid phosphatases from n. Crassa. Resumos. 1991 ;[citado 2025 dez. 30 ] -
Vancouver
Han SW, Barbosa JE, Rossi A, Michelin MA. Biochemical and immunological characterization of acid phosphatases from n. Crassa. Resumos. 1991 ;[citado 2025 dez. 30 ] - Purification and constitutive excretion of acid phosphatase in neurospora crassa
- Constitutive secretion of alkaline phosphatase in Neurospora crassa
- The synthesis of phosphate-repressible alkaline phosphatase do not appear to be regulated by ambient pH in the filamentous mould Neurospora crassa
- Anti-peptide antibody detecting a neo-antigen on the cri stump left on erythrocytes after proteolysis
- Expressão do receptor para complemento tipo 1(CR1) em eritrócitos de pacientes com leishmaniose visceral
- Complement receptor type 1 (CRI) expression on erythrocytes of patients with kala-azar
- Phage display as a novel promising antivenom therapy: a review
- Anticorpo antipeptidio capaz de detectar fragmentos do receptor crl ligado a eritrocitos humanos, apos proteolise
- It is increased carriage on red cell c'R IND.1' and not solubilization that is the main function of complement in the handling of immunocomplexes
- Production of human monoclonal antibothropic scFv isolated from a nonimmunized phage library
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