A Novel Method for the N-Terminal Modification of Native Proteins

Bioconjugate Chemistry

Volumn 15, Issue 2, 2004, Pages 231-234

  Lewinska, Marzena ^a   Seitz, Christian ^a   Skerra, Arne ^a   Schmidtchen, Franz P ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCONJUGATES; KINETICALLY CONTROLLED; N TERMINUS; N-TERMINAL SEQUENCES; N-TERMINALS; NATIVE PROTEINS; NON-DESTRUCTIVE CONDITIONS; NOVEL METHODS; REGIOSELECTIVE MODIFICATION; TERMINAL MODIFICATIONS;

PROTEINS;

ALANINE; IMMUNOGLOBULIN A; IMMUNOGLOBULIN A PROTEINASE; PROLINE; PROTEIN; PROTEINASE; UNCLASSIFIED DRUG; WATER;

AMINO TERMINAL SEQUENCE; ARTICLE; CONJUGATE; CONJUGATION; KINETICS; PROTEIN DEGRADATION; PROTEIN MODIFICATION; STEREOCHEMISTRY; TECHNIQUE;

EID: 1642353533     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc034085f     Document Type: Article

References (21)

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20. em = 350 nm). At the concentration maximum of the product after 3 h, the reaction was quenched by acidification and the product was isolated by HPLC and analyzed by MALDI-TOF mass spectroscopy and Edman degradation.
21. Recombinant IgA-protease was purchased from MoBiTec, Göttingen, Germany. The enzyme is quite sensitive and was preconditioned in the reaction buffer for 1 h after thawing from the frozen state. The activity was standardized using the hydrolysis of BOC-Pro-Arg-Pro-Pro-p-nitroanilide (to be published). According to our procedure, commercial samples of IgA-protease contained 2.5-6 U/μg protein.