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ผลงานตีพิมพ์ในวารสารวิชาการThe Role of Lectins in Finfish: A Reviewผู้แต่ง: Elumalai, P., Rubeena, A.S., Arockiaraj, J.,  Dr.Ratree Wongpanya, Associate Professor , Cammarata, M., Ringรธ, E., Vaseeharan, B., วารสาร:  
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ผลงานตีพิมพ์ในวารสารวิชาการComparative transcriptomic analysis reveals genes encoding polygalacturonase inhibitors and lectins as promising candidates conferring bruchid (Callosobruchus chinensis) resistance in moth bean (Vigna aconitifolia)ผู้แต่ง:Gamage, S.I.R., Takahashi, H., Bui, K.T., Nakazono, M., Dr.Prakit Somta, Associate Professor , วารสาร: |
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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Inhibitory Effects of Mulberry Leaf Lectins to Silkworm Proteases) ผู้เขียน:ดร.สุนันทา รัตนาโภ, รองศาสตราจารย์ , Yuwadee Thawalvichit, ดร.อมรรัตน์ พรหมบุญ, รองศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractProteases from digestive fluid of Nang-lai strains of the Thai silkworm, Bombyx mori were partially purified by 40% ammonium sulfate fractionation and p-aminobenzidine agarose affinity chromatography. Six proteases named P1-P6 were obtained and P4, P5 and P6 were purified approximately 21,18 and 17 folds, respectively. The P4, P5 and P6 proteases had an equal apparent subunit molecular weight of 24 kDa and native molecular weight of 66 kDa. They exhibited the alkaline optimum pH at pH 9.0, 11.0 and 11.5, respectively. Their proteolytic activities were inhibited by specific trypsin inhibitors including leupeptin, tyrosyl-L-lysine chloromethylketone and soybean trypsin inhibitor suggesting that they were trypsin-like proteases. Inhibitory effect of two lectins from mulberry leaf, MLL1 and MLL2, to the proteases were studied. It was found that MLL1, in comparison to MLL2 and ConA, had greater inhibitory effects towards the protease P4 and a lesser inhibitory effect towards the protease P5 and P6. The inhibition of the proteases by both mulberry leaf lectins was not recovered by the specific lectinbinding sugars, N-glycolylneuraminic acid and N-acetylgalactosamine. |
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หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Lectins Histochemical Studies in Submandibular Salivary Gland of the House Musk Shrew, Suncus murinus) ผู้เขียน:ดร.อภินันท์ สุประเสริฐ, ศาสตราจารย์ , Sahathep JUNTARAVIMOL, Pibul Ruensupapichat, ดร.ดลดา ศรีใส, อาจารย์, ดร.เสรี กุญแจนาค, ผู้ช่วยศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractSubmandibular glands of male house musk shrew, Suncus murinus, were examined by light microscopic histochemical methods. The staining procedures employed were horseradish peroxidase conjugated lectins, Alcian blue (AB) pH 1.0, AB pH 2.5, Periodic acid-Schiff (PAS) and AB pH2.5-PAS in combination with enzyme digestion with neuraminidase. The lectins used in the present study were Peanut agglutinin (PNA), Dolichos biflorus agglutinin (DBA), Wheat germ agglutinin (WGA), Limax flavus agglutinin (LFA), Ulex europaeus agglutinin-I (UEA-I), and Loutus tetragonolobus agglutinin (LTA) The submandibular gland of Suncus murinus is a branched tubuloacinar gland. Its secretory endpiece contains both serous and mucous cells. Granular ducts, modified striated ducts, were found to be well developed. All the mucous acinar cells were colored deep blue with the AB pH 2.5-PAS procedure and were stained strongly with LFA. Neuraminidase digestion changed the deep blue coloration with the AB pH 2.5-PAS procedure to light red and abolished all staining of mucous cells with LFA. Removal of sialic acid with neuraminidase imparted weak to strong affinity for PNA. Serous cells showed strong red coloration with the AB pH2.5-PAS procedure and were reacted strongly with PNA, DBA and WGA. Granular duct cells exhibited moderate reaction with PAS, LTA and UEA-I. |
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ที่มา:การประชุมนักวิจัยรุ่นใหม่พบเมธีวิจัยอาวุโส สกว. ครั้งที่ 11หัวเรื่อง:การศึกษายีน C-type lectin ในกุ้งกุลาดำ |
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