Isolation and characterization of a human alternative complement pathway-inhibiting protein from larval hemolymph of the silkworm, Bombyx mori
| Autor: | T Maenaka, Yasutaka Sekijima, Tetsuo Hiyama, A Uda, Yuriko Fujikura |
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| Rok vydání: | 2000 |
| Předmět: |
Erythrocytes
Immunology Complement Pathway Alternative Molecular Sequence Data Hemolysis Classical complement pathway Bombyx mori Hemolymph Animals Humans Amino Acid Sequence Peptide sequence chemistry.chemical_classification Base Composition Complement Inactivator Proteins Sheep biology Dose-Response Relationship Drug fungi Amino-Terminal Amino Acid biology.organism_classification Bombyx Molecular biology Amino acid Complement system Molecular Weight chemistry Biochemistry Larva Alternative complement pathway Insect Proteins Electrophoresis Polyacrylamide Gel Rabbits Developmental Biology |
| Zdroj: | Developmental and comparative immunology. 25(2) |
| ISSN: | 0145-305X |
| Popis: | An alternative complement pathway-inhibiting protein (ACPIP), which inhibits the activation of the alternative complement pathway (ACP) of the human serum, was isolated from larval hemolymph of the silkworm, Bombyx mori, by using ammonium sulfate fractionation and column chromatographies to homogeneity. About 400microg of ACPIP was routinely obtained from 20ml hemolymph. The purified ACPIP preparation consisted of two distinct polypeptides (34 and 32kDa) on SDS-PAGE. The amino acid compositions of the two polypeptides were nearly identical; 21% of the amino acid residues were acidic. The amino terminal amino acid sequences up to 20 residues in these two polypeptides were also identical. Addition of the ACPIP to human serum resulted in a dose-dependent inhibition of the hemolysis of intact rabbit erythrocytes via the ACP, whereas in no inhibition of hemolysis of sensitized-sheep erythrocytes (EA) via the classical pathway. |
| Databáze: | OpenAIRE |
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