Part 1: 為了探討疏水性或電荷在αA-水晶體蛋白第71位置上對分子伴護的效應，我們比較分析αA-水晶體蛋白野生種和在N-端帶有的額外11個殘基包含六個組氨酸(His)標示的兩個穾變種F71W 和 F71R蛋白質的活性。在誘導胰島素聚集的實驗中顯示，這額外11個殘基對類伴護活性影響很小。 F71W突變種的活性和野生種蛋白相似；而F71R的活性卻明顯的降低。 F71W及野生種之活性隨莫耳數之增加而增加,然而 F71R 之活性卻隨著莫耳數之增加而急速減少。ANS 發射螢光的測量顯示 F71R 有最高的表面疏水性，推測可能是在這個位置上的正電荷造成立體組態的改變而使疏水性增加。熱穩定性實驗亦觀察到因疏水性的增加，而導致高分子量聚集的形成 (>2000 KDa)。 在熱穩定性的研究顯示F71W 比F71R及野生種較具熱穩定性。在不同溫度對類伴護活性的實驗研究中顯示，單體及寡聚合體 (650 kDa) 是造成伴護官能的主要因素，而表面疏水性並不是伴護活性存在的必要條件。近紫外光圓二色光譜的實驗研究顯示 β-摺板型結構（β-sheet） 是所有三個水晶體蛋白二級結構的主要成份及 F71R 具有高百分比的任意型結構（random coil）。
part 2: 從快速生長的芽鞘中，有一分子量為15 kDa 的Bowman-Birk 蛋白酶抑制劑(BBIrc)已經被純化，且利用部分N 端序列定
序、液相層析-質譜儀（LC-MS）和基質輔助雷射脫附游離飛行時間質譜儀（MALDI-TOF MS），已鑑定出其為一133 胺基酸多肽鏈（BBIrc1）。酵素動力學研究指出，此蛋白酶抑制劑對胰蛋白酶表現出競爭性的抑制，其解離常數為4.0 x 10-7M，而對α-胰凝乳蛋白酶表現為非競爭性的抑制，其解離常數為9.3 x 10-7 M。西方墨點法的結果顯示，由15 kDa 蛋白製備而成的抗血清，會分別辨識15 kDa 和另一25 kDa 的蛋白質。在有氧和低氧條件下15 kDa 蛋白的表現量幾乎維持恆定；然而，當快速伸長的芽鞘由低氧移至有氧環境時，25 kDa蛋白的表現會隨時間之增加而提升，這結果顯示稻米芽鞘BBI 蛋白的表現模式與發育過程中的形態變化有關。25 kDa
蛋白前9 個氨基酸的部分N 端序列為AEAPPRPPK 和 RBBI3-1 的第37 至45 序列相同，且在液相層析串聯質譜研究亦發現有分子量的片段符合於RBBI3-1。此25 kDa 蛋白也與牛之胰蛋白酶(Bovine trypsine)有專一性結合，這蛋白質之表現模式首次發現:「氧氣」能選擇性地增加特定BBI 基因表現，本研究結果表示稻米芽鞘中BBI 蛋白質可能扮演著多重生物性功能。

Part 1: In order to explore whether hydrophobicity or charge at 71th residue is important for chaperone-like activity, wild type (wt) and two mutant αA-crystallins, F71W and F71R, with extra 11 residues including 6 histidines tagged at the N-terminal were prepared. Chaperone-like activity toward dithiotreitol (DTT) induced insulin aggregation showed the 11 extra residues had little effect. The activity for F71W was as active as the wild type; while F71R was much less active. For wild type and F71W, the activity increased with the increase of molar quantity; surprisingly, for F71R it caused a drastic decline. ANS fluorescence measurements showed F71R had the highest surface hydrophobicity, suggesting positive charge at this site caused the conformational alteration leading to the increase of hydrophobicity and this hydrophobicity resulted in the formation of high molecular weight aggregates (>2000 kDa) observed from the thermal stability study. Thermal stability study revealed F71W was the most thermally stable crystallin. Chaperone-like activity studies at various temperature suggested the monomer and oligomer, 650 kDa, were responsible for chaperone function and surface hydrophobicity was not the prerequisite for activity. Near-UV CD studies showed β-sheet was the major secondary structure for all three crystallins and F71R had higher percentage of random coil.
part 2: A 15 kDa rice Bowman-Birk inhibitor from fast elongating coleoptiles has been purified and identified using partial N-terminal sequence, LC-MS, and MALDI-TOF MS as a 133 amino acid polypeptide (BBIrc1). The kinetic study shows this protease inhibitor displays competitive inhibition toward trypsin with Ki of 4.0 x 10-7 M and non-competitive inhibition toward α-chymotrypsin with Ki of 9.3 x 10-6 M. The Western blotting results of the anti-sera raised against this 15 kDa protein showed that this anti-serum recognized two BBI proteins with molecular size around 15 kDa (BBIrc1) and 25 kDa (BBIrc2) and the quantity of the expression of 15 kDa was nearly constant under both aerobic and hypoxia conditions; however, the 25 kDa expression was greatly up-regulated when the fast elongating coleoptiles were transferred from hypoxia conditions to the aerobic conditions. The results indicate that the expression pattern of BBIs proteins correlated to the developmental stage in terms of morphological changes. The partial N-terminal sequence of the first 9 amino acids of 25 kDa was AEAPPRPPK, which has the same amino acid sequence of 37th to 45th of RBBI3-1 and LC-MS study shows that several mass fragments fit to RBBI3-1. The 25 kDa protein also shows specific binding to bovine trypsin.
This expression pattern demonstrates for the first time that environmental factor, oxygen, can select and enhance specific BBI gene expression. The results of this study suggest BBI proteins might play multiple biological functions inside rice coleoptiles.

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