کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10801095 | 1054728 | 2005 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biochemical characterization of an effective substrate and potent activators of CK2 copurified with Bowman-Birk-type proteinase inhibitor from soybean seeds in vitro
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کلمات کلیدی
STIA-kinaseC-kinaseBBICK2CK1SbiEGCGDTTSDS-PAGE - الکتروفورز ژل پلی آکریل آمیدsodium dodecylsulfate polyacrylamide gel electrophoresis - الکتروفورز ژل پلی اکریللید سدیم دودسیل سولفاتdithiothreitol - دیتیوتریتولsoybean trypsin inhibitor - مهارکننده تریپسین سویاcAMP-dependent protein kinase - پروتئین کیناز وابسته به cAMPcasein kinase 1 - کازئین کیناز 1Casein kinase 2 - کازئین کیناز 2high-performance liquid chromatography - کروماتوگرافی مایعی کاراHPLC - کروماتوگرافی مایعی کارا
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
By means of Mono P column chromatography, an effective phosphate acceptor (EPA) of casein kinase 2 (CK2) was purified from the Bowman-Birk-type proteinase inhibitor (BBI) fraction of soybean seeds. The most acidic EPA (aEPA, pI = approx. 3.7) was heavily phosphorylated when incubated with CK2 and 5 μM [γ-32P]ATP in the presence of poly-Arg (a CK2 activator) in vitro. However, aEPA was slightly phosphorylated by casein kinase 1 (CK1) as effective as C-kinase and not at all by A-kinase in vitro. The 13 N-terminal amino acid residues (SDHSSSDDESSKP) of aEPA were 100% homologous to the corresponding sequence of soybean BBI-type proteinase inhibitor CII (SBI CII). Polyamine at 3 mM stimulated 4.6-fold the CK2-mediated phosphorylation of aEPA, and this phosphorylation was sensitive to quercetin (ID50 = approx. 0.1 μM) in vitro. Furthermore, two basic proteins [Mr = 29,000 (p29) and 17,000 (p17)] copurified with BBI were identified as proteolytic cleavage products of basic 7S globulin and functioned as potent CK2 activators in vitro. aEPA fully phosphorylated by CK2 in the presence of poly-Arg or basic proteins formed a complex with trypsin, whereas unphosphorylated aEPA was digested by trypsin in vitro. These results suggest that (i) aEPA (a BBI isoform) may coexist with two basic proteins (p29 and p17) generated from basic 7S globulin; and (ii) the physiological interaction between aEPA and its binding trypsin-like proteinases may be regulated through specific phosphorylation of aEPA by CK2 activated with the two basic proteins in legume seeds.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 1, 30 August 2005, Pages 47-56
Journal: Biochimica et Biophysica Acta (BBA) - General Subjects - Volume 1725, Issue 1, 30 August 2005, Pages 47-56
نویسندگان
Tayo Katano, Yayoi Kamata, Takashi Ueno, Teisuke Furuya, Takeshi Nakamura, Kenzo Ohtsuki,