نتایج جستجو برای: mannose binding protein mbp

تعداد نتایج: 1452875  

ژورنال: :مجله علوم پزشکی رازی 0
صنم نامی نامی مهربان فلاحتی فریده زینی لامع اخلاقی محمد صدری فاطمه طباطبائی زینب قاسمی

زمینه و هدف : درماتوفیتوزیس یک بیماری قارچی جلدی شایع با انتشار جهانی است . اینترلوکین 8 ( il8 ) آزاد شده از کراتینوسیت ها در حضور آنتی ژن های درماتوفیتی سبب القاء پاسخ حاد در عفونت درماتوفیتی می شود و متعاقبا تولید پروتئین های فاز حاد توسط سلول های کبدی رخ می دهد . crp ( c-reactive protein ) و mbl ( mannose-binding lectin ) از پروتئین های فاز حاد هستند . تحقیقات اندکی در مورد پروتئین های فاز ح...

2017
Sang Beum Lee Sung Kwon Park Yong Soo Kim

Myostatin (MSTN) is a potent negative regulator of skeletal muscle growth. MSTN propeptide (MSTNpro) inhibits MSTN binding to its receptor through complex formation with MSTN, implying that MSTNpro can be a useful agent to improve skeletal muscle growth in meat-producing animals. Four different truncated forms of pig MSTNpro containing N-terminal maltose binding protein (MBP) as a fusion partne...

Journal: :Protein expression and purification 2006
Mark I Donnelly Min Zhou Cynthia Sanville Millard Shonda Clancy Lucy Stols William H Eschenfeldt Frank R Collart Andrzej Joachimiak

Production of milligram quantities of numerous proteins for structural and functional studies requires an efficient purification pipeline. We found that the dual tag, his(6)-tag-maltose-binding protein (MBP), intended to facilitate purification and enhance proteins' solubility, disrupted such a pipeline, requiring additional screening and purification steps. Not all proteins rendered soluble by...

2000
Donald M. Miller

Myc-binding protein-1 (MBP-1) is a 37-kDa protein with sequence homology to the 3* portion of the a-enolase gene. a-Enolase is a 48-kDa protein, which plays a critical role in the glycolytic pathway. MBP-1 binds to the c-myc P2 promoter and down-regulates c-myc expression. We have investigated the role of a-enolase in regulation of the c-myc protooncogene. RNase protection assay shows that a-en...

Journal: :The Biochemical journal 1989
R A Childs K Drickamer T Kawasaki S Thiel T Mizuochi T Feizi

Oligosaccharide recognition by three mammalian mannose-binding proteins was investigated by using as probes a series of structurally characterized neoglycolipids in t.l.c. binding assays. The neoglycolipids were derived from N-linked oligosaccharides of complex, high-mannose and hybrid types and from human milk oligosaccharides and simple di- and tri-saccharides. The three proteins, namely the ...

Journal: :Fermentation 2023

Aspartate ammonia-lyase (AAL) catalyzes the reversible conversion reactions of aspartate to fumaric acid and ammonia. In this work, Lactobacillus paracasei LpAAL gene was heterologously expressed in Escherichia coli. As well as a recombinant His-tagged protein, maltose-binding protein (MBP) fused used enhance its solubility expression level. Both proteins showed broad substrate specificity, cat...

Journal: :Protein and peptide letters 2007
J Caine I Volitakis R Cherny J Varghese I Macreadie

The 42 amino acid Alzheimer's Abeta peptide has been produced in E. coli as a soluble fusion to maltose binding protein (MBP). Affinity purification on amylose columns of MBP-Abeta and MBP led to the recovery of proteins at purities that were suited for physicochemical analyses. MBP-Abeta was able to bind approximately 2 mole equivalents of copper or 4 mole equivalents of zinc, while MBP alone ...

Journal: :The Journal of Experimental Medicine 1990
R Malhotra S Thiel K B Reid R B Sim

A receptor binding to the C1q subcomponent of complement has been reported by many workers. In this paper we report for the first time that C1q receptor binds not only to C1q, but also to three other structurally similar ligands, namely mannan binding protein (MBP), conglutinin, and lung surfactant protein (SP-A). All these ligands have been reported to enhance removal of species bound to their...

Journal: :Nature chemical biology 2013
Eunkyung Kim Sanghwa Lee Aram Jeon Jung Min Choi Hee-Seung Lee Sungchul Hohng Hak-Sung Kim

Protein dynamics have been suggested to have a crucial role in biomolecular recognition, but the precise molecular mechanisms remain unclear. Herein, we performed single-molecule fluorescence resonance energy transfer measurements for wild-type maltose-binding protein (MBP) and its variants to demonstrate the interplay of conformational dynamics and molecular recognition. Kinetic analysis provi...

Journal: :The Journal of biological chemistry 1985
M D Manson W Boos P J Bassford B A Rasmussen

Maltose-binding protein (MBP) is essential for maltose transport and chemotaxis in Escherichia coli. To perform these functions it must interact with two sets of cytoplasmic membrane proteins, the MalFGK transport complex and the chemotactic signal transducer Tar. MBP is present at high concentrations, on the order of 1 mM, in the periplasm of maltose-induced or malTc constitutive cells. To det...

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