Reactivation of lysozyme from inactive HNB-lysozyme

Reiss, Anita; Lukton, A.

doi:10.1016/0045-2068(75)90021-8

Cited by 8 publications

(2 citation statements)

References 23 publications

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“…More recently (216,320) it has been found that the HNB-group linked at the indole nucleus of tryptophan in a protein can be reversibly removed. REiss and LuKTON (320) studied the reaction of HNB-Br with Iysozyme and found that the formation of HNB-lysozyme resulted in enzyme inactivation by modification of one tryptophan residue.…”

Section: Ni3~c(ch)mentioning

confidence: 98%

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The Chemistry of Tryptophan in Peptides and Proteins

Fontana¹,

Toniolo²

1976

Fortschritte Der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products

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Section: Ni3~c(ch)mentioning

confidence: 98%

“…However, it was found that when HNB-Iysozyme was kept at pH 2.8 for several hours, the modified enzyme regained its activity, although not completely, and formation of HNB-OH was noticed. This fact would imply that regeneration of Iysozyme activity is related to reversible modification of the 62-tryptophan residue (320).…”

Section: Ni3~c(ch)mentioning

confidence: 99%

The Chemistry of Tryptophan in Peptides and Proteins

Fontana¹,

Toniolo²

1976

Fortschritte Der Chemie Organischer Naturstoffe / Progress in the Chemistry of Organic Natural Products

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Investigation of the interaction between enzyme and inhibitor by the combination of chemical modification, electrospray ionization mass spectrometry and frit-fast atom bombardment liquid chromatography/mass spectrometry

Akashi

Niitsu

Yuji

et al. 1993

Biol. Mass Spectrom.

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The interaction between enzyme and its inhibitor, hen egg-white lysozyme and tri-N-acetylglucosamine (NAG3), was studied by the combination of chemical modification, enzymatic digestion, electrospray ionization mass spectrometry and frit-fast atom bombardment liquid chromatography/mass spectrometry. Chemical modification of amino groups, carboxyl groups, and indole groups was carried out independently. In the absence of NAG3, the carboxyl group in Asp 101 was modified by glycinamidation, and the indole group in Trp 62 was modified by Koshland reagent. In the presence of NAG3, the degree of modification of Asp 101 and Trp 62 decreased. It is suggested that Asp 101 and Trp 62 are involved in the interaction with NAG3. The result is consistent with the one obtained by x-ray crystallography. It is indicated that the combination of chemical modification and mass spectrometry may be effective for the investigation of the binding reaction of enzyme to inhibitor and of protein-protein interaction.

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