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Chemical modification of amino acid residues in glycerinatedVorticella stalk and Ca2+-induced contractility

✍ Scribed by Kono, Rin-Ichiro ;Ochiai, Tsutomu ;Asai, Hiroshi

Publisher: John Wiley and Sons
Year: 1997
Tongue: English
Weight: 69 KB
Volume: 36
Category: Article
ISSN: 0886-1544
DOI: 10.1002/(sici)1097-0169(1997)36:4<305::aid-cm1>3.0.co;2-4

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✦ Synopsis

The glycerinated stalk of the peritrich ciliate Vorticella, was treated with various reagents to chemically modify the amino acid residues. The influences of these modifications on spasmoneme contractility were investigated. First, it was confirmed that the spasmoneme contraction is not inhibited by alteration of SH groups. It was also demonstrated that chemical modification of methionine and tryptophan residues abolishes spasmoneme contractility. The reagents used for chemical modification were N-bromosuccinimide (NBS), chloramine T, and 2-hydroxy-5-nitrobenzyl bromide (HNBB), which abolished spasmoneme contractility at concentrations of 40-50 µM, 200-300 µM, and 4 mM, respectively. These results suggest that, along with Ca 21 binding proteins, there are other as yet to be identified proteins involved in contractility. Cell Motil.

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