کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1976335 1060684 2006 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Purification and some properties of two creatine kinase isoforms from herring (Clupea harengus) spermatozoa
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Purification and some properties of two creatine kinase isoforms from herring (Clupea harengus) spermatozoa
چکیده انگلیسی

Creatine kinase (CK, EC 2.7.3.2) isoforms play important role in energy homeostasis and together with easily diffusible compounds like creatine and phosphocreatine maintain a cellular energy buffer and intracellular energy transport system. The CK activity in spermatozoa is the highest from all studied tissues in herring. It was detected that the two CK isoforms, CK1 and CK2, are characteristic only for spermatozoa and are not expressed in other herring tissues. Isolation and purification procedures allowed obtaining purified enzymes with specific activity of the 345 μmol/min/mg for CK1 and 511 μmol/min/mg for CK2. Native Mr's of the CK1 and CK2 determined by gel permeation chromatography were about 330,000 and 90,000, respectively. These results indicate that CK1 form has octameric structure and CK2 is a dimer mostly characteristic for cytosolic CK enzymes. In immunoblotting studies with antisera against CK2, the response was observed for CK2 and there was no response for CK1 and two other isoforms from herring skeletal muscle. These findings make the herring isoforms an interesting model for studies on the fish CK biochemical properties.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology - Volume 144, Issue 2, June 2006, Pages 152–158
نویسندگان
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