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 Biochemjournal_title
Journal of biochemistryauthors
Takeda S,Yamaki M,Ebina S,Nagayama Kdoi
10.1093/jb/117.2.267subject
Has Abstractpub_date
1995-02-01 00:00:00pages
267-70issue
2eissn
0021-924Xissn
1756-2651journal_volume
117pub_type
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