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1.
Sesame peptide powder (SPP) exhibited angiotensin I-converting enzyme (ACE) inhibitory activity, and significantly and temporarily decreased the systolic blood pressure (SBP) in spontaneously hypertensive rats (SHRs) by a single administration (1 and 10 mg/kg). Six peptide ACE inhibitors were isolated and identified from SPP. The representative peptides, Leu-Val-Tyr, Leu-Gln-Pro and Leu-Lys-Tyr, could competitively inhibit ACE activity at respective Ki values of 0.92 μM, 0.50 μM, and 0.48 μM. A reconstituted sesame peptide mixture of Leu-Ser-Ala, Leu-Gln-Pro, Leu-Lys-Tyr, Ile-Val-Tyr, Val-Ile-Tyr, Leu-Val-Tyr, and Met-Leu-Pro-Ala-Tyr according to their content ratio in SPP showed a strong antihypertensive effect on SHR at doses of 3.63 and 36.3 μg/kg, which accounted for more than 70% of the corresponding dosage for the SPP-induced hypotensive effect. Repeated oral administration of SPP also lowered both SBP and the aortic ACE activity in SHR. These results demonstrate that SPP would be a beneficial ingredient for preventing and providing therapy against hypertension and its related diseases.  相似文献   

2.
Angiotensin I-converting enzyme (ACE) inhibitory activity was generated from elastin and collagen by hydrolyzing with thermolysin. The IC50 value of 531.6 µg/mL for ACE inhibition by the elastin hydrolysate was five times less than 2885.1 µg/mL by the collagen hydrolysate. We confirmed the antihypertensive activity of the elastin hydrolysate in vivo by feeding spontaneously hypertensive rats (male) on a diet containing 1% of the elastin hydrolysate for 9 weeks. About 4 week later, the systolic blood pressure of the rats in the elastin hydrolysate group had become significantly lower than that of the control group. We identified novel ACE inhibitory peptides, VGHyp, VVPG and VYPGG, in the elastin hydrolysate by using a protein sequencer and quadrupole linear ion trap (QIT)-LC/MS/MS. VYPGG had the highest IC50 value of 244 µM against ACE and may have potential use as a functional food.  相似文献   

3.
Peptides showing inhibitory activity against the angiotensin I-converting enzyme (ACE) were investigated from the fibroin fraction of discarded silk fabric. Fibroin, which was hydrolyzed with alcalase after partial hydrolysis with hot aqueous 40% CaCl2, released two major active peptides showing ACE-inhibitory activity. The two peptides were identified as glycyl-valyl-glycyl-tyrosine (GVGY) and glycyl-valyl-glycyl-alanyl-glycyl-tyrosine (GVGAGY) by analyses with a protein sequencer and LC/MS/MS. GVGY, whose ACE-inhibitory activity has not previously been reported, showed a blood pressure-depressing effect on spontaneously hypertensive rat (SHR).  相似文献   

4.
采用蔗糖密度梯度离心法对钝顶螺旋藻光合膜蛋白(PSI)进行分离纯化,并对其光谱学性质、热稳定性及光合放氧活性进行分析表征。结果发现,采用蔗糖密度精度离心法,可以成功分离出4条色素蛋白质复合体条带,其中最下层条带为完整的PSI三聚体,其每毫克叶绿素a光合放氧活性达到420μmol/h。当温度达到50℃左右时,分离得到的PSI在溶液开始变性失活。  相似文献   

5.
普通小球藻对嗪草酮、骠马和甲草胺的敏感性研究   总被引:9,自引:1,他引:8  
通过96h的毒性实验,研究了普通小球藻对3种不同作用机制农田常用除草剂嗪草酮、骠马和甲草胺的敏感性.结果表明。在实验条件下,嗪草酮、甲草胺对普通小球藻的毒性随时间的推移有加重趋势。并呈现很好的剂量效应关系;最高抑制生长浓度(嗪草酮0.24mg·L^-1,甲草胺12.8mg·L^-1)处理组的最大比增长率分别为对照组的12.38%和31.58%;骠马低浓度对普通小球藻的抑制作用不明显,并呈一定的生长促进效应,0.08mg·L^-1浓度组普通小球藻最大比增长率为对照组的111.44%,而高浓度则具有明显的生长抑制作用,并随时间推移,毒性逐渐减弱.嗪草酮、骠马和甲草胺的96hEC50分别为0.021、0.937和5.54mg·L^-1.普通小球藻对嗪草酮最敏感。其次为骠马和甲草胺.3种除草剂在实验条件下对普通小球藻叶绿素a含量的影响和对普通小球藻生长的影响相似。表现出较好的剂量.效应关系.  相似文献   

6.
为探索浮游动物和藻类之间可能存在的信息传递,研究了萼花臂尾轮虫培养滤液对铜绿微囊藻、斜生栅藻和小球藻的生长及群体形成的影响.把萼花臂尾轮虫按1000个·L-1的初始密度置于小球藻中培养24h后,用孔径0.15μm的微孔滤膜抽滤,得到轮虫培养滤液,此滤液中含有轮虫在生活过程中释放的一些信息化学物质.将轮虫培养滤液以20%的比例分别加入纯培养的铜绿微囊藻、斜生栅藻和小球藻中,进行为期7d的试验.结果表明,萼花臂尾轮虫培养滤液能显著地促进斜生栅藻的群体形成,而对铜绿微囊藻和小球藻在群体形成方面没有显著作用.另外,该滤液能显著提高小球藻种群的增长,对铜绿微囊藻和斜生栅藻的生长无明显影响.3种藻类对萼花臂尾轮虫的潜在牧食采取了不同的生态策略:斜生栅藻形成群体,增大摄食阻力,从而降低被摄食的风险;小球藻通过提高增长率来抵消被取食的损失;铜绿微囊藻是通过其它方式来降低被牧食(例如毒素).这些方式分别是这些藻类维持种群规模的反牧食防御策略之一.  相似文献   

7.
Soluble carbonic anhydrase (CA, EC 4.2.1.1) inducible by low levels of CO2 was purified from the unicellular green alga Chlorella sorokiniana grown at alkaline pH. The purified CA had a specific activity of 2,300 units (mg protein)−1. The molecular mass of the CA was found to be 100 kDa by non-dissociating (native)-polyacrylamide gel electrophoresis and 50 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The 50-kDa subunit was recognized by concanavalin A. These results suggest that the protein has a dimeric form with two 50-kDa subunits that are glycosylated in an asparagine-linked manner. The native CA was revealed by isoelectric focusing to be a very acidic protein with an isoelectric point of 4.2. About 60% of the CA activity was inhibited by 0.5 M NaCl. The enzyme was inactivated over 95% by preincubation with 50 mM dithiothreitol but not with 1 mM dithiothreitol. After partial amino acid sequence analysis, a cDNA clone of the CA was isolated and characterized. The cloned cDNA fragment encoded a 348-amino-acid polypeptide (36,709 Da) including an NH2-terminal hydrophobic signal peptide composed of 35 amino acids (3,725 Da). Conserved regions of sequences found in animal CAs, in the periplasmic (pCA) and the intracellular CAs of Chlamydomonas, and in the plasma-membrane-bound CA of Dunaliella (Dca) were also found in this Chlorella CA. The signal sequence was significantly homologous to the pCA and the Dca. The internal signal sequence between the large and the small subunits reported for pCA was not found in this Chlorella CA. The soluble CA of this alga was an α-type CA with salt-sensitive, periplasm-locating and acidic properties and very different from pCA and Dca with their salt-sensitive/neutral and salt-resistant/acidic properties, respectively. Received: 25 May 1998 / Accepted: 9 July 1998  相似文献   

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