title: Probing of L-arginine as an additive for the temperature-induced aggregation of veterinary growth hormones: fluorescence study.
abstract: The influence of L-arginine on the temperature-induced aggregation of porcine and mink growth hormones was studied by fluorescence spectroscopy. It was found that L-arginine suppresses the heat-induced aggregation. Moreover, the analysis of L-arginine interaction with the native proteins by fluorescence spectroscopy and circular dichroism spectroscopy revealed no significant changes in their native structure. On the basis of the results, L-arginine could be considered as a potential additive for the prevention of storage and temperature-related denaturation and aggregation of veterinary growth hormones.
authors.affiliation: Department of Chemistry and Bioengineering, Faculty of Fundamental Sciences, Vilnius Gediminas Technical University, Sauletekio al. 11, LT-10223, Vilnius-40, Lithuania.
authors.forename: Andrejus
authors.initials: A
authors.lastname: Cirkovas
authors.forename: Jolanta
authors.initials: J
authors.lastname: Sereikaite
mesh_terms: D000818:Animals; D001120:Arginine / Q000737:chemistry*; D002942:Circular Dichroism / Q000379:methods; D013006:Growth Hormone / Q000737:chemistry*; D006358:Hot Temperature; D008907:Mink; D011489:Protein Denaturation; D017434:Protein Structure, Tertiary; D013050:Spectrometry, Fluorescence; D013552:Swine
chemical_list: D013006:Growth Hormone; D001120:Arginine