Isolation and characterization of an aspartic protease from salpichroa origanifolia fruits

This report describes the purification of an aspartic protease (salpichroin) from ripe fruits of Salpichroa origanifolia (Solanaceae) starting with precipitation using organic solvents and anionexchange chromatography with 32.1% recovery and 13.4-fold purification. SDS-PAGE and zymograms of this enz...

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Detalles Bibliográficos
Autores principales: Rocha, G.F., Obregón, W.D., Muñoz, F., Guevara, M.G., Fernández, G., Rosso, A.M., Parisi, M.G.
Formato: JOUR
Materias:
Caseinolytic activity
Peptide mass fingerprinting
Plant aspartic protease
Purification
Salpichroa origanifolia
Salpichroin
1,10 phenanthroline
aspartic proteinase
benzylsulfonyl fluoride
casein
chymosin
edetic acid
hemoglobin
n [n (3 carboxyoxirane 2 carbonyl)leucyl]agmatine
pepstatin
synthetic peptide
insulin
amino acid sequence
anion exchange chromatography
Article
controlled study
enzyme kinetics
fruit
matrix assisted laser desorption ionization time of flight mass spectrometry
molecular weight
nonhuman
pH
polyacrylamide gel electrophoresis
precipitation
protein analysis
protein cleavage
protein hydrolysis
protein isolation
protein purification
Solanaceae
chemistry
isolation and purification
molecular genetics
Amino Acid Sequence
Aspartic Acid Proteases
Fruit
Insulin
Molecular Sequence Data
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_09298665_v22_n4_p379_Rocha
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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