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ผลงานตีพิมพ์ในวารสารวิชาการPurification, Characterization, and Crystallization of Crocodylus siamensis Hemoglobinผู้แต่ง: Jandaruang, J, Siritapetawee, J, Songsiriritthigul, C,  Dr.Sutthidech Preecharram, Lecturer , Azuma, T, Dhiravisit, A, Fukumori, Y, Thammasirirak, S, วารสาร: 
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ผลงานตีพิมพ์ในวารสารวิชาการการศึกษาฮีโมโกลบินของสุนัขพันธุ์ไทยบางแก้วโดยเจลฟิลเตชันคอลัมน์โครมาโตกราฟฟี (2015)ผู้แต่ง:Dr.Jatuporn Rattanasrisomporn (Noosud), Associate Professor, Mrs.Amornrate Sastravaha, Associate Professor , Mr.wirat nimitsuntiwong, Associate Professor, สิทธิรักษ์ รอยตระกูล, สุวิช, Dr.Autchara Kayan, Assistant Professor , Dr.chaiwat Boonkaewwan, Assistant Professor , วารสาร: |
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 หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Biochemical Properties of Nile Tilapia (Oreochromis niloticus) Hemoglobin) ผู้เขียน:เกรียงไกร ทองสาร, ดร.วันชัย วรวัฒนเมธีกุล, รองศาสตราจารย์ , ดร.สุริยัน ธัญกิจจานุกิจ, ผู้ช่วยศาสตราจารย์ , นางชูศรี ศรีเพ็ญ, ผู้ช่วยศาสตราจารย์, ดร.อาภัสสรา ชูเทศะ, รองศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractHemoglobins of O. niloticus (averaged standard length of 18.07 ? 0.89 cm and weight of 216.86 ? 27.13 g) were analysed of some biochemical properties. Average hematocrits were 25.80 ? 3.71% and average hemoglobin concentrations were 7.05 ? 1.08 g/dl. It was found that there were 9 – 11 types of hemoglobin by cellulose acetate electrophoresis. The anodic and cathodic hemoglobins were revealed by native polyacrylamide gel electrophoresis with approximate amounts of 45.72 and 54.28% of total hemoglobin, respectively. In addition, the cathodic hemoglobin was classified by cellulose acetate electrophoresis as cathodic I and cathodic II with approximate amounts of 47.62 and 6.66% of total hemoglobin, respectively. Mass spectrometry was performed to determine molecular weights of hemoglobin. It was found that the molecular weights of native hemoglobin was 63.0 kDa and the molecular weights of subunits were 15.3, 15.6 and 16.1 kDa. The pIs of anodic and cathodic hemoglobins ranged 5.28 – 6.80 and 7.27 – 9.71 , respectively. |
หัวเรื่อง:ไม่มีชื่อไทย (ชื่ออังกฤษ : Identification and Characterization of Hemoglobin in Thai Bangkaew Dogs using Chromatographic,Electrophoretic and Mass Spectrometric Techniques) ผู้เขียน:ดร.จตุพร รัตนศรีสมพร (หนูสุด), รองศาสตราจารย์, Sittiruk Roytrakul, ดร.ชัยวัฒน์ บุญแก้ววรรณ, ผู้ช่วยศาสตราจารย์, ดร.อาภัสสรา ชูเทศะ, รองศาสตราจารย์ สื่อสิ่งพิมพ์:pdf AbstractThe present study was aimed to measure the hematocrit (Ht) and the hemoglobin (Hb) concentration of Thai Bangkaew dogs, to investigate Hb phenotypes based upon the electrophoretic pattern of the Hb and to estimate molecular weights of the Hb (tetramer) and Hb subunits using gel filtration chromatography, SDS-PAGE and MALDI-TOF/TOF MS. The results showed that 30 dogs had a mean Ht value (? standard error of the mean) of 36.38 ? 0.77% and a mean Hb concentration (? standard error of the mean) of 13.10 ? 0.32 g/dL. In addition, the fraction obtained from gel filtration of Sephadex G-100, at pH 7.4, corresponding to the isolated Hb protein was estimated at a molecular weight of 65,956 Dalton. The Hb fraction was used for analysis by native polyacrylamide gel electrophoresis (native-PAGE), sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF/TOF MS). The Hb electophoretic mobility in native-PAGE showed that all samples had one two-banded phenotype, consisting of a low mobility major band (94%) and a minor fast band (6%). In addition, SDS-PAGE showed two distinct bands of approximate molecular weights 12,980 and 14,820 Dalton, respectively. Moreover, the MALDI-TOF/TOF MS analyzes on the purified Hb fraction exhibited two abundant mass peaks at the molecular weights of 15,194.78 and 15,946.66 Dalton and three minor peaks at the molecular weights of 32,020.53, 48,326.29 and 64,545.95 Dalton. |