Ko, Eun
(Department of Bioengineering and Biotechnology, College of Engineering, Chonnam National University)
,
Ku, Seul-I
(Interdisciplinary Program of Bioenergy and Biomaterials Graduate School (BK21 Plus Program), College of Engineering, Chonnam National University)
,
Kim, Dae-yoon
(Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology)
,
Shin, Sooim
(Interdisciplinary Program of Bioenergy and Biomaterials Graduate School (BK21 Plus Program), College of Engineering, Chonnam National University)
,
Choi, Moonsung
(Department of Optometry, College of Energy and Biotechnology, Seoul National University of Science and Technology)
Lysozyme is an antibacterial enzyme that is found in most of body fluids. Lysozyme in tears plays a primary role in protecting eye from harmful environments; if lysozyme is degraded or inhibited, eyes are likely to be more vulnerable to bacterial infection. In this study, lysozyme activity was evalu...
Lysozyme is an antibacterial enzyme that is found in most of body fluids. Lysozyme in tears plays a primary role in protecting eye from harmful environments; if lysozyme is degraded or inhibited, eyes are likely to be more vulnerable to bacterial infection. In this study, lysozyme activity was evaluated according to varying concentrations of heavy metals, copper, zinc, cobalt and manganese and light metal, calcium that are frequently found in airborne particulate matters and was assayed using a dye-quenching lysozyme substrate, Micrococcus lysodeikticus. Less fluorescence intensity was observed with increasing amounts of copper, zinc, manganese and cobalt but not with calcium suggesting that these metals have some affinity with lysozyme and inhibit lysozyme activity. When albumin, the second most common protein in tears, was added on the reaction of lysozyme and metals, lysozyme activity was partially restored. This finding suggests that the albumin might protect damage caused by metals on lysozyme. To identify whether the decrease in enzymatic activity was related to structural changes of lysozyme, SDS-PAGE was conducted and only with copper did lysozyme show marked smearing bands on the SDS-gel, meaning that copper degraded lysozyme consistent with the sharpest activity decrease.
Lysozyme is an antibacterial enzyme that is found in most of body fluids. Lysozyme in tears plays a primary role in protecting eye from harmful environments; if lysozyme is degraded or inhibited, eyes are likely to be more vulnerable to bacterial infection. In this study, lysozyme activity was evaluated according to varying concentrations of heavy metals, copper, zinc, cobalt and manganese and light metal, calcium that are frequently found in airborne particulate matters and was assayed using a dye-quenching lysozyme substrate, Micrococcus lysodeikticus. Less fluorescence intensity was observed with increasing amounts of copper, zinc, manganese and cobalt but not with calcium suggesting that these metals have some affinity with lysozyme and inhibit lysozyme activity. When albumin, the second most common protein in tears, was added on the reaction of lysozyme and metals, lysozyme activity was partially restored. This finding suggests that the albumin might protect damage caused by metals on lysozyme. To identify whether the decrease in enzymatic activity was related to structural changes of lysozyme, SDS-PAGE was conducted and only with copper did lysozyme show marked smearing bands on the SDS-gel, meaning that copper degraded lysozyme consistent with the sharpest activity decrease.
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문제 정의
PM has long been studied in a variety of fields and is closely related to daily life and health. The findings from this study reflect this trend and particularly regarding the effects of heavy metals on lysozyme. There have been many studies on the interaction between metals and proteins, but this is the first attempt to reveal how heavy metals influence lysozyme in the presence of albumin.
참고문헌 (20)
Jaishankar, Monisha, Tseten, Tenzin, Anbalagan, Naresh, Mathew, Blessy B., Beeregowda, Krishnamurthy N..
Toxicity, mechanism and health effects of some heavy metals.
Interdisciplinary toxicology,
vol.7,
no.2,
60-72.
Erie, Jay C., Butz, John A., Good, Jonathan A., Erie, Elizabeth A., Burritt, Mary F., Cameron, J. Douglas.
Heavy Metal Concentrations in Human Eyes.
American journal of ophthalmology,
vol.139,
no.5,
888-893.
Merlini, Giampaolo, Bellotti, Vittorio.
Lysozyme: A paradigmatic molecule for the investigation of protein structure, function and misfolding.
Clinica chimica acta,
vol.357,
no.2,
168-172.
Erie, Jay C., Butz, John A., Good, Jonathan A., Erie, Elizabeth A., Burritt, Mary F., Cameron, J. Douglas.
Heavy Metal Concentrations in Human Eyes.
American journal of ophthalmology,
vol.139,
no.5,
888-893.
Quiterio, Simone Lorena, Sousa da Silva, Célia Regina, Arbilla, Graciela, Escaleira, Viviane.
Metals in airborne particulate matter in the industrial district of Santa Cruz, Rio de Janeiro, in an annual period.
Atmospheric environment,
vol.38,
no.2,
321-331.
Zereini, F., Alt, F., Messerschmidt, J., Wiseman, C., Feldmann, I., von Bohlen, A., Muller, J., Liebl, K., Puttmann, W..
Concentration and Distribution of Heavy Metals in Urban Airborne Particulate Matter in Frankfurt am Main, Germany.
Environmental science & technology,
vol.39,
no.9,
2983-2989.
Croguennec, Thomas, Nau, Françoise, Molle, Daniel, Le Graet, Yvon, Brule, Gérard.
Iron and citrate interactions with hen egg white lysozyme.
Food chemistry,
vol.68,
no.1,
29-35.
Jing, M., Song, W., Liu, R..
Binding of copper to lysozyme: Spectroscopic, isothermal titration calorimetry and molecular docking studies.
Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy,
vol.164,
103-109.
Ikeda K, and HAMAGUCHI K. Interactions of Mn2+, Co2+, and Ni2+ions with hen egg-white lysozyme and with its Nacetylchitooligosaccharide complexes. J Biochem 1973;73:307-322.
Li, Shu Jie.
Structural details at active site of hen egg white lysozyme with di‐ and trivalent metal ions.
Biopolymers,
vol.81,
no.2,
74-80.
Stabili, L., Pagliara, P..
Effect of zinc on lysozyme-like activity of the seastar Marthasterias glacialis (Echinodermata, Asteroidea) mucus.
Journal of invertebrate pathology,
vol.100,
no.3,
189-192.
Yonath, A., Smilansky, A., Sharon, N..
X-ray crystallographic study of binding of cobalt ion to hen egg-white lysozyme.
FEBS letters,
vol.49,
no.2,
178-180.
Gallo, A.A., Swift, T.J., Sable, H.Z..
Magnetic resonance study of the Mn2+ - lysozyme complex.
Biochemical and biophysical research communications,
vol.43,
no.6,
1232-1238.
Lu, Jin, Stewart, Alan J., Sadler, Peter J., Pinheiro, Teresa J.T., Blindauer, Claudia A..
Albumin as a zinc carrier: properties of its high-affinity zinc-binding site.
Biochemical Society transactions,
vol.36,
no.6,
1317-1321.
Bal, W., Sokolowska, M., Kurowska, E., Faller, P..
Binding of transition metal ions to albumin: Sites, affinities and rates.
Biochimica et biophysica acta, General subjects,
vol.1830,
no.12,
5444-5455.
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