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undergraduate thesis
Uloga kalpaina u proteolizi mišićnog tkiva
Osijek: Josip Juraj Strossmayer University of Osijek, Department of Chemistry, 2010. urn:nbn:hr:182:860432
Rak, Ivana
Josip Juraj Strossmayer University of Osijek
Department of Chemistry
Department of General, Inorganic and Physical Chemistry and Methodology of Chemistry

Institutional repository: Repository of the Department of Chemistry, Osijek

Cite this document

Rak, I. (2010). Uloga kalpaina u proteolizi mišićnog tkiva (Undergraduate thesis). Osijek: Josip Juraj Strossmayer University of Osijek, Department of Chemistry. Retrieved from https://urn.nsk.hr/urn:nbn:hr:182:860432

Rak, Ivana. "Uloga kalpaina u proteolizi mišićnog tkiva." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, 2010. https://urn.nsk.hr/urn:nbn:hr:182:860432

Rak, Ivana. "Uloga kalpaina u proteolizi mišićnog tkiva." Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, 2010. https://urn.nsk.hr/urn:nbn:hr:182:860432

Rak, I. (2010). 'Uloga kalpaina u proteolizi mišićnog tkiva', Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, accessed 04 January 2025, https://urn.nsk.hr/urn:nbn:hr:182:860432

Rak I. Uloga kalpaina u proteolizi mišićnog tkiva [Undergraduate thesis]. Osijek: Josip Juraj Strossmayer University of Osijek, Department of Chemistry; 2010 [cited 2025 January 04] Available at: https://urn.nsk.hr/urn:nbn:hr:182:860432

I. Rak, "Uloga kalpaina u proteolizi mišićnog tkiva", Undergraduate thesis, Josip Juraj Strossmayer University of Osijek, Department of Chemistry, Osijek, 2010. Available at: https://urn.nsk.hr/urn:nbn:hr:182:860432

Metadata
TitleUloga kalpaina u proteolizi mišićnog tkiva
Title (english)The role of calpains in muscle tissue proteolysis
AuthorIvana Rak
MentorElizabeta Has Schon (mentor)
Committee memberElizabeta Has Schon (predsjednik povjerenstva)
GranterJosip Juraj Strossmayer University of Osijek
Department of Chemistry
(Department of General, Inorganic and Physical Chemistry and Methodology of Chemistry)
Osijek
Defense date and country2010-11-19, Croatia
Scientific / art field,
discipline and subdiscipline		NATURAL SCIENCES
Chemistry
Abstract
Kalpainski enzimski sustav čine dvije sveprisutne proteaze, μ-kalpaina i m-kalpaina, te njihov inhibitor, kalpastatin. Kalpaini su heterodimeri koji se sastoje od dvije podjedinice: velike katalitičke veličine 80 kDa organizirane u četiri domene, te male regulatorne veličine 30 kDa organizirane u dvije domene. Na temelju dosadašnjih saznanja o katalitičkim svojstvima kalpaina, aktivnost kalpaina se regulira koncentracijom Ca2+, autproteolizom, kalpastatinom, staničnom lokalizacijom i specifičnim područjem aktivnog mjesta. Kalpaini sudjeluju u različitim staničnim procesima uključujući staničnu mobilnost, prijenos signala, stanični ciklus, apoptozu, patološke bolesti i postmortalnu proteolizu. Mehanizam posmortalne proteolize mesa je vrlo složen proces u kojem sudjeluje velik broj različitih enzima. Glavnu ulogu u miofibrilarnoj proteolizi imaju kalpaini. Miofibrilarna žilavost posljedica je mrtvačke ukočenosti, dok je miofibrilarno omekšavanje uzrokovano cijepanjem miofibrilarnih proteina kalpainima. Na temelju važnih dosadašnjih dokaza, razjašnjeni su mnogi faktori koji utječu mekoću mesa.
Abstract (english)
The calpain system consist of calpains, a family of Ca2+ dependent cysteine proteases whose members are expressed ubiquitously or in a tissue-specific way. Calpains are heterodimeric proteins, composed of catalytic subunit of about 80 kDa organised in 4 domains and the small 30 kDa subunit organised in 2 domains. Based on the current knowledge of the catalytic properties of the calpains, it seems that calpain activity is regulated by Ca2+ concentration, calpastatin, intracellular location and subsite specificity of the calpains. Calpains participate in a variety of cellular processes including cell motility, signal transduction pathways, the cell cycle, apoptosis, long-term potentiation, pathological states in cells and postmortem proteolysis. The exact mechanisms involved in the postmortem meat tenderization process are complex and includes a large number of different enzymes. The main myofibrillar proteolysis can be attributed to calpains. The myofibrillar toughness is considered to be affected by the development of rigor-mortis and tenderization caused by calpains break-down of the contractile proteins. Based on the relevant evidence thus far obtained, factors affecting meat tenderness, although not fully understood, are in perspective to be clarified.
Keywords
Keywords (english)
Languagecroatian
URN:NBNurn:nbn:hr:182:860432
Study programmeTitle: Chemistry
Study programme type: university
Study level: undergraduate
Academic / professional title: sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije (sveučilišni/a prvostupnik/prvostupnica (baccalaureus/baccalaurea) kemije)
Type of resourceText
File originBorn digital
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Created on2016-06-07 06:56:59