دورية أكاديمية
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The first trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae was found in Dendrobium pendulum: purification, characterization, and effects of stress factors.

التفاصيل البيبلوغرافية
العنوان: The first trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae was found in Dendrobium pendulum: purification, characterization, and effects of stress factors.
المؤلفون: Siripipatthana P; Department of Biochemistry, Faculty of Science, Khon Kaen University, Muang, Khon Kaen, 40002, Thailand., Phaonakrop N, Roytrakul S, Senawong G, Mudalige-Jayawickrama RG, Sattayasai N
المصدر: Plant cell reports [Plant Cell Rep] 2015 Jul; Vol. 34 (7), pp. 1253-62. Date of Electronic Publication: 2015 Apr 19.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Germany NLM ID: 9880970 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1432-203X (Electronic) Linking ISSN: 07217714 NLM ISO Abbreviation: Plant Cell Rep Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Berlin ; New York : Springer, 1981-
مواضيع طبية MeSH: Protein Multimerization*/drug effects , Stress, Physiological*/drug effects, Dendrobium/*chemistry , Lectins/*isolation & purification , Mannose-Binding Lectins/*chemistry , Plant Lectins/*chemistry, Amino Acid Sequence ; Base Sequence ; DNA, Complementary/genetics ; Electrophoresis, Polyacrylamide Gel ; Hot Temperature ; Lectins/chemistry ; Lectins/metabolism ; Mannose-Binding Lectin/metabolism ; Mannose-Binding Lectins/isolation & purification ; Mannose-Binding Lectins/metabolism ; Mercaptoethanol/pharmacology ; Molecular Sequence Data ; Plant Lectins/isolation & purification ; Plant Lectins/metabolism ; Reference Standards ; Sequence Homology, Amino Acid
مستخلص: Key Message: Trimeric Galanthus nivalis agglutinin-related lectin of Orchidaceae with two conformational forms was first studied in Dendrobium pendulum . It was highly expressed by stress factors. Using mannan-agarose column chromatography, a mannose-binding protein was purified from Dendrobium pendulum Roxb. pseudobulb. After heating in the presence of sodium dodecyl sulfate (SDS) with or without 2-mercaptoethanol, the protein showed one band with molecular mass of 14.0 kDa on SDS-polyacrylamide gel electrophoresis (PAGE). Without heating, three bands were found at positions of 14.0, 39.4, and 41.5 kDa, but a higher amount of 39.4 and 41.5 kDa protein bands were seen in the presence of 2-mercaptoethanol. Liquid chromatography-tandem mass spectrometry and database search indicated that the 14.0 kDa protein band contained three peptide fragments identical to parts of a lectin precursor from Dendrobiu m findleyanum Parish & Rchb.f. Native-PAGE and Ferguson plot showed that the purified protein had two native forms with molecular masses of 44.2 and 45.3 kDa, indicating three 14.0 kDa polypeptide subunits. The purified protein exhibited the agglutination activity with trypsinized chicken erythrocytes. It was then recognized as a Galanthus nivalis agglutinin-related lectin and named D. pendulum agglutinin (DPA). Using reverse transcription-polymerase chain reaction and DNA sequencing, the deduced amino acid sequence of DPA precursor showed the highest homology (96.4%) with a lectin precursor of D. findleyanum and contained three mannose-binding sites. Greater amounts of DPA were found when the pseudobulbs were treated with stress factors including ultraviolet light, abscisic acid, hydrogen peroxide, and acetylene gas.
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المشرفين على المادة: 0 (DNA, Complementary)
0 (Lectins)
0 (Mannose-Binding Lectin)
0 (Mannose-Binding Lectins)
0 (Plant Lectins)
0 (snowdrop lectin)
60-24-2 (Mercaptoethanol)
تواريخ الأحداث: Date Created: 20150421 Date Completed: 20160310 Latest Revision: 20200930
رمز التحديث: 20221213
DOI: 10.1007/s00299-015-1785-x
PMID: 25893876
قاعدة البيانات: MEDLINE
الوصف
تدمد:1432-203X
DOI:10.1007/s00299-015-1785-x