Effect of zinc salts on the structure–function of actomyosin from pelagic fish

Autor:	Parigi Ramesh Kumar, Sijo Mathew, B. A. Shamasundar, V. Prakash
Rok vydání:	2009
Předmět:	chemistry.chemical_classification biology Chemical structure ATPase chemistry.chemical_element Bioengineering Zinc Applied Microbiology and Biotechnology Biochemistry Enzyme assay Enzyme chemistry Myosin Biophysics biology.protein Solubility Protein secondary structure
Zdroj:	Process Biochemistry. 44:704-709
ISSN:	1359-5113
DOI:	10.1016/j.procbio.2009.02.018
Popis:	The effect of zinc salts, zinc chloride and zinc sulfate on the structure and ATPase enzyme activity of actomyosin from pelagic fish (Sardinella longiceps) has been investigated. ATPase enzyme activity decreased in the presence of both the zinc salts. The inhibitory effect is present in both pH of 7.0 and 9.0. At concentration of 1נ10-3M of zinc salts, complete inhibition of ATPase enzyme activity is observed. With the increase in temperature from 25C to 45C the ATPase activity decreased by nearly 80%. The solubility profile of actomyosin in the presence of zinc salts shows a sigmoid pattern as the concentration of both the zinc salts increases. Free SH content of actomyosin decreased with the increase in concentration of zinc salts. Intrinsic fluorescence indicated significant decrease in relative fluorescence intensity of actomyosin. This indicates significant alterations in the structure of actomyosin. Analysis of secondary structure also indicates significant alteration in the [alpha]-helical content upon binding of both zinc salts.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0187eb69b3a76654beb945292d3a4e15 https://doi.org/10.1016/j.procbio.2009.02.018 Zobrazit plný text záznamu Full Text from ScienceDirect