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Studies on the Chemical Modification of Goat Liver Cystatin and the Effect on Its Anti-Papain Inhibitory Activity

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Abstract

Goat liver cystatin was subjected to various chemical modifications in order to ascertain the amino acid residues responsible for its structural and functional integrity. Modification of tryptophan by HNBB led to the complete inactivation of the protein. The inactivation was also accompanied by the complete loss of tryptophan fluorescence at 340 nm. The reaction of liver cystatin with HNBB yielded a characteristic decrease in absorbance at 280 nm. Acetylation of the amino groups of liver cystatin was carried out in the presence of acetic anhydride. The acetylated cystatin showed a decrease in fluorescence intensity at 335 nm which could be attributed to the modification of tyrosine residue due to side reaction.

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Authors and Affiliations

  1. Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, 202002, India

    Aaliya Shah, Mohammad Aatif, Medha Priyadarshini, Fakhra Amin & Bilqees Bano

  2. Department of Biochemistry, King Saud University, Riyadh, Saudi Arabia

    Mohd Shahnawaz Khan

Authors
  1. Aaliya Shah
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  2. Mohammad Aatif
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  3. Medha Priyadarshini
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  4. Mohd Shahnawaz Khan
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  5. Fakhra Amin
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  6. Bilqees Bano
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Correspondence to Bilqees Bano.

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Shah, A., Aatif, M., Priyadarshini, M. et al. Studies on the Chemical Modification of Goat Liver Cystatin and the Effect on Its Anti-Papain Inhibitory Activity. J Fluoresc 22, 1627–1632 (2012). https://doi.org/10.1007/s10895-012-1106-5

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  • DOI: https://doi.org/10.1007/s10895-012-1106-5

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