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<span style="font-size:12.0pt;font-family: "Times New Roman";mso-fareast-font-family:"Times New Roman";mso-ansi-language: EN-IN;mso-fareast-language:EN-IN;mso-bidi-language:AR-SA" lang="EN-IN">Nature of <i style="mso-bidi-font-style:normal">o</i>-phthalaldehyde reaction with pigeon liver fatty acid synthetas</span>

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Title Nature of o-phthalaldehyde reaction with pigeon liver fatty acid synthetas
 
Creator Mukherjee, Sanchita
Katiyar, Sarvagya S
 
Description 63-68
Pigeon liver fatty acid synthetase (FAS) was inactivated
irreversibly by stoichiometric concentration of o-phthalaldehyde exhibiting a bimolecular kinetic process.
FAS-o-phthalaldehyde adduct gave a characteristic absorption maxima at 337 nm. Moreover
this derivative showed fluorescence emission maxima at 412 nm when excited at
337 nm. These results were consistent with isoindole ring formation in which
the -SH group of cysteine and ε-NH2, group of lysine participate in
the reaction. The inactivation is caused by the reaction of the
phosphopantetheine -SH group since it is protected by either acetyl- or malonyl-CoA.
The enzyme incubated with iodoacetamide followed by o-phthalaldehyde showed no change in fluorescence

intensity but decrease in intensity was found in
the treatment of 2,4,6-trinitrobenzenesulphonic acid (TNBS), a lysine specific reagent
with the enzyme prior to o-phthalaldehyde
addition. As o-phthalaldehyde did not
inhibit enoyl-CoA reductase activity, so nonessential lysine is involved in the
o-phthalaldehyde reaction. Double
inhibition experiments showed that 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB),
a thiol specific reagent, binds to the san1e cysteine which is also involved in
the o-phthalaldehyde reaction.
Stoichiometric results indicated that 2 moles of o-phthalaldehyde were incorporated per mole of enzyme molecule upon
complete inactivation.
 
Date 2012-12-31T19:05:40Z
2012-12-31T19:05:40Z
1999-04
 
Type Article
 
Identifier 0975-0959 (Online); 0301-1208 (Print)
http://hdl.handle.net/123456789/15426
 
Language en_US
 
Rights CC Attribution-Noncommercial-No Derivative Works 2.5 India
 
Publisher NISCAIR-CSIR, India
 
Source IJBB Vol.36(2) [April 1999]