首页> 外文期刊>Neuropeptides: An International Journal >Investigation of inhibition angiotensin-converting enzyme (ACE) activity and opioid activity of two hemorphins, LVV-hemorphin-5 and VV-hemorphin-5, isolated from a defined peptic hydrolysate of bovine hemoglobin.
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Investigation of inhibition angiotensin-converting enzyme (ACE) activity and opioid activity of two hemorphins, LVV-hemorphin-5 and VV-hemorphin-5, isolated from a defined peptic hydrolysate of bovine hemoglobin.

机译:从限定的牛血红蛋白消化性水解物中分离的两种血红素,LVV-hemorphin-5和VV-hemorphin-5的抑制血管紧张素转换酶(ACE)活性和阿片类药物活性的研究。

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摘要

Two peptides, LVV-hemorphin-5 and VV-hemorphin-5, were isolated from a defined peptic bovine hemoglobin hydrolysate by reversed-phase HPLC. These peptides were identified as 31-38 and 32-38 fragments of beta chain of bovine hemoglobin. Their inhibitory activity towards angiotensin-converting enzyme and opioid potency were determined. Since their amino acid sequences show close homology with spinorphin, which is found in human cerebrospinal fluid and in the bovine spinal cord, the possible physiological role in vivo of these peptides was discussed.
机译:通过反相HPLC从确定的消化性牛血红蛋白水解物中分离出两种肽,LVV-hemorphin-5和VV-hemorphin-5。这些肽被鉴定为牛血红蛋白β链的31-38和32-38片段。确定了它们对血管紧张素转化酶的抑制活性和阿片样物质的效力。由于它们的氨基酸序列与在人脑脊髓液和牛脊髓中发现的菠菜啡具有紧密的同源性,因此讨论了这些肽在体内可能的生理作用。

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