Proteolytic hydrolysis and purification of the LRP/alfa-2-macroglobulin receptor domain from ?-macroglobulins

A new, easier and efficient purification method, using Sephacryl and DEAE-Sephacel, of the C-terminal fragment of two ?-macroglobulins, ?2-M and PZP, is presented. Two larger peptides were identified for each protein as the C-terminal fragment, with molecular weights of ?30 kDa and the N-terminal se...

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Autores:
Tipo de recurso:
Fecha de publicación:
2007
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22891
Acceso en línea:
https://doi.org/10.1016/j.pep.2006.12.008
https://repository.urosario.edu.co/handle/10336/22891
Palabra clave:
Alpha 2 macroglobulin
Chymotrypsin
Low density lipoprotein receptor related protein
Monoclonal antibody
Peptide fragment
Placenta protein
Proteinase
Unclassified drug
Amino acid sequence
Article
Chemistry
Enzyme linked immunosorbent assay
Female
Human
Hydrolysis
Isolation and purification
Metabolism
Molecular genetics
Molecular weight
Polyacrylamide gel electrophoresis
Pregnancy
Protein tertiary structure
Sequence analysis
Time
Western blotting
Alpha-macroglobulins
Amino acid sequence
Chymotrypsin
Endopeptidases
Enzyme-linked immunosorbent assay
Female
Humans
Hydrolysis
Ldl-receptor related protein 1
Molecular sequence data
Molecular weight
Peptide fragments
Pregnancy
Pregnancy proteins
Time factors
?-macroglobulins
C-terminal region
Chymotrypsin
Pzp
polyacrylamide gel
western
tertiary
protein
monoclonal
human
Pzp protein
Antibodies
Blotting
Electrophoresis
Protein structure
Sequence analysis
Rights
License
Abierto (Texto Completo)