臺灣博碩士論文加值系統

中 文 摘 要
草蝦(Penaeus monodon)血淋巴(hemolymph)中的凝固蛋白(clottable protein)可經由兩次的陰離子交換樹脂(DEAE-anion exchanger) 純化得到，純化的凝固蛋白在加入鈣離子及蝦血球溶出液(hemocyte lysate supernatant)後可聯結成大分子，它的分子量經SDS-PAGE和MALDI-TOF mass spectrometry測定為 380 kDa，它是由兩個190 kDa 次單元所組成，草蝦凝固蛋白的分子量大小和胺基酸組成(amino acid composition) 和N端的胺基酸序列(N-terminal amino acid sequence)與龍蝦(spiny lobster, Panulius interruptus)和螯蝦(crayfish, Pacifastacus leniusculus) 的凝固蛋白相似，草蝦凝固蛋白可被醣類染劑染色(PAS stain)，可確定草蝦凝固蛋白是一種醣蛋白(glycoprotein)，經由醣類組成分析(carbohydrate analysis)，它含有2.6%甘露糖(mannose)和1.2% N-乙醯半乳糖胺(N-acetylglucosamine) ，經由Endoglycosidase H切割後分析草蝦凝固蛋白上的寡醣(oligosaccharide)，主要為Man8GlcNAc和Man9GlcNAc的醣鍊(sugar chains)所組成，它的結構在 66 0C以下相當穩定，它的二級結構經由圓振二向色性(circular dichroism)分析，主要由44% a-helices 、26% b sheets和16% b turn所組成，而它的二級結構在0.1 M ~0.5 M NaCl和pH 4~9的緩衝液(buffer)中都相當的穩定。
將純化的凝固蛋白經CNBr，Lys-C和Glu-C切割成小的peptide，經由C18管柱層析(C18 column chromatography)分離，利用分離peptide的胺基酸序列與N端的胺基酸序列設計引子(primer)進行去氧核醣核酸聚合酵素鏈鎖反應(polymerase chain reaction) ，經選殖獲得一段500 bp DNA，具有正確的胺基酸序列，以這段cDNA充當探針(probe)，篩選草蝦cDNA library，同時利用草蝦凝固蛋白的抗體篩選草蝦的cDNA library，總共獲得5個clones組成完整的草蝦凝固蛋白cDNA，草蝦凝固蛋白的cDNA為含有6,124 個鹼基對(bp)，內含1,670個胺基酸其中包括14個胺基酸的signal sequence，將草蝦凝固蛋白胺基酸序列與基因資料庫的基因進行胺基酸序列比對，發現草蝦凝固蛋白胺基酸序列與螯蝦(crayfish, Pacifastacus leniusculus) 的凝固蛋白胺基酸序列具有36%的相同性(57%的相似性) ，草蝦凝固蛋白胺基酸序列和昆蟲的卵黃前質(vitellogenin) 胺基酸序列有17-20%的相同性(50%的相似性)，而在草蝦凝固蛋白的C端與昆蟲卵黃前質的C端的胺基酸序列比對，發現十個cysteine與一個GI/LCG motif是保存在相同的位置，因此推測草蝦凝固蛋白的基因是由卵黃前質演化而來，而草蝦凝固蛋白胺基酸序列和apolipoprotein B具有相同性，同時與具有D domain的脊椎動物von Willebrand Factor和mucin 2和家蠶(Bombyx mori) hemocytin的蛋白質均具有相同性，顯示這些基因具有相似的演化結果。草蝦凝固蛋白為轉醯胺酵素(transglutaminase)的受質(substrate)，推測草蝦凝固蛋白中胺基酸序列5個重複的SKTS (197-231) 、Gln-rich的區域(1079-1122)及poly Q (1635-1650)這三個區域可能為TGase作用的位置，參與凝固蛋白分子的鍵結(cross-linking)。
對於草蝦凝固蛋白的生合成組織以西方墨點法(Western Blot) 、北方轉印法(Northern blot)和免疫組織化學法(immunohistochemistry)進行檢測，發現草蝦凝固蛋白在中鰓(gill)、心臟(heart)、肝胰臟(hepatopancreas) 、類淋巴器官(lymphoid organ)和肌肉(muscle) 均有表現(expression)，以鰓和心臟的表現最高，其次為類淋巴器官和肝胰臟，肌肉則表現最少，僅血球細胞(hemocyte)則完全沒有表現。

Abstract
The clottable protein was purified from the hemolymph of tiger shrimp (Penaeus monodon) by sequential DEAE-anion exchanger chromatography. The protein formed stable clots in the presence of Ca2+ and the transglutaminase contained in hemocyte lysate. The molecular mass of the clottable protein was determined to be 380 kDa by SDS-PAGE and MALDI-TOF mass spectrometry and the protein is a disulfide-linked homodimer. By PAS stain, the clottable protein was found to be a glycoprotein. The size and the amino acid composition and sequences of the clottable protein are similar to those of other crustaceans including lobster (Panulirus interruptus) and crayfish (Pacifastacus leniusculus). The clottable protein was found to contain 2.6% mannose and 1.2% N-acetylglucosamine. Endoglycosidase H digestion of the glycoprotein generated mainly Man8GlcNAc and Man9GlcNAc sugar chains, suggesting the presence of high-mannose type glycan structure. Its conformation is stable at temperature below 66 0C, as shown by UV-spectrophotometry. The protein contains 44% a-helices, 26% b sheets and 16% b turn as determined by circular dichroism spectra. Its conformation is stable in buffers of pH 4-9 and NaCl concentration up to 0.5 M.
The purified clottable protein was subjected to CNBr cleavage and Glu-C and Lys-C digestion. The peptides were separated by C18 column chromatography. We designed the degenrate primers from the peptide sequences and N-terminal sequence. PCR were performed with the synthetic primers and the total cDNA as template. We obtained a 500 bp clone encoding authentic amino acid sequences of the clottable protein. Moreover, the cDNA expression library was constructed and screened with the antiserum and the PCR product. We totally obtained 5 clones. These five clones were isolated and sequenced to complete the entire nucleotide sequence of the clottable protein. The complete cDNA coding for the entire protein is 6,124 base pairs in length and has an open reading frame encoding a protein of 1,670 amino acids, including a 14-amino acid signal peptide. Upon conducting a protein sequence database survey, the shrimp clottable protein shows 36% identities to the crayfish clotting protein and up to 20% identities to members of insect vitellogenins. In the C-terminal 200 residues of the clottable protein as well as of the insect vitellogenins there are 10 cysteines residues and a GICG motif in concensus, suggestive of genetic relationship between these genes. The clottable protein also contains a stretch with similarity to the D domain of mammalian von Willebrand factor, mucin 2 and silkworm hemocytin. A region rich in Gln residues (1079-1122), a polyGln motif (1635-1650) and five Ser-Lys-Thr-Ser repeats (197-231) are present in the shrimp protein, suggesting these regions might be involved in cross-linking of the clottable proteins in the presence of TGase.
The tissue distribution of clottable protein was detecteded by Western blot, immunohistochemistry and Northern blot analysis. The clottable protein is expressed in most of the shrimp tissue. The expression of the clottable protein is found with highest level in gill and heart of the shrimp, with a lower level in lymphoid organ, hepatopancreas and muscle but not in hemocytes.

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目錄
中文摘要
英文摘要
前　　言
材料與方法
討　　論
參考文獻
附　　圖
附　　表
附　　錄

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