Site-specific reactivities of cysteine residues in horse L-apoferritin.

Abstract:

:Recombinant horse L-apoferritin and its mutants were used to compare the reactivities of two different cysteinyl residues with 7-fluoro-4-sulfamoyl-2,1,3-benzoxadiazole (ABD-F), p-chloromercuribenzoic acid (PCMB), N-(9-acridinyl)maleimide (NAM), and 4-maleimido-2,2,6,6-tetramethylpiperidine-N-oxyl (NEM-TEMPO). ABD-F selectively reacted with cysteine 52 (C52), which is located on the inner surface of the peptide shell of apoferritin. In contrast, PCMB reacted only with cysteine 130 (C130), which is located at the 3-fold channels of the shell. NAM and NEM-TEMPO reacted with both C52 and C130.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Takeda S,Yamaki M,Ebina S,Nagayama K

doi

10.1093/jb/117.2.267

subject

Has Abstract

pub_date

1995-02-01 00:00:00

pages

267-70

issue

2

eissn

0021-924X

issn

1756-2651

journal_volume

117

pub_type

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