Please use this identifier to cite or link to this item:
https://cuir.car.chula.ac.th/handle/123456789/60431
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | อภิชาติ กาญจนทัต | - |
dc.contributor.other | จุฬาลงกรณ์มหาวิทยาลัย. สถาบันวิจัยเทคโนโลยีชีวภาพและวิศวกรรมพันธุศาสตร์ | - |
dc.date.accessioned | 2018-10-08T07:58:32Z | - |
dc.date.available | 2018-10-08T07:58:32Z | - |
dc.date.issued | 2557 | - |
dc.identifier.uri | http://cuir.car.chula.ac.th/handle/123456789/60431 | - |
dc.description | เนื้อเรื่องภาษาอังกฤษ | en_US |
dc.description.abstract | Blood pressure regulation is partially dependent on the renin-angiotensin system; renin acts on angiotensinogen to release angiotensin-I, which is further converted into the angiotensin II by the angiotensin I-converting enzyme (ACE). ACE plays a key physiological role in the regulation of blood pressure by virtue of two different reactions that it catalyzes: conversion of the inactive angiotensin I to the powerful vasoconstrictor angiotensin II, and inactivation of the vasodilator bradykinin. Crude extract and ammonium sulphate cut protein extracts, and their pepsin-pancreatin hydrolysates, from the seeds of 4 Thai fruits (i) Carica papaya L.; (papaya; unripen and ripen form), (ii) Nephelium lappaceum L. (rambutan) (iii) Dimocarpus longan Lour. subsp. (longan), and (iv) Litchi chinensis Sonn. (lychee) were screened for their in vitro angiotensin I- converting enzyme inhibitory (ACEI) activity. The protein hydrolysate of lychee seeds shows the highest potential of ACE inhibitory activity at IC50 value 0.22±0.010 mg protein/ml. The protein hydrolysate of unripen papaya seeds, longan seeds, and lychee seeds show uncompetitive and non-competitive inhibition with Ki values at 6.02, 2.82, and 5.62 mg protein/ml, with optimum pH in range of 6-8. After partial purification with ultrafiltration technique, UF-3 (below 5 kDa) of longan seeds show the highest inhibitory activity with IC50 values at 0.43±0.011 mg protein/ml. This fraction was subjected to RP-HPLC and five peaks were separated, and subjected to LC/MS/MS for amino acids sequences analysis. The P1-F1, P3-F1, and P3-F4 show the most inhibitory activity. | en_US |
dc.description.sponsorship | ได้รับทุนอุดหนุนการวิจัยจากงบประมาณแผ่นดิน ประจำปี 2557 (GRB_BSS_79_57_61_11) | en_US |
dc.language.iso | en | en_US |
dc.publisher | จุฬาลงกรณ์มหาวิทยาลัย | en_US |
dc.rights | จุฬาลงกรณ์มหาวิทยาลัย | en_US |
dc.subject | Protein hydrolysates | en_US |
dc.subject | Angiotensin I | en_US |
dc.title | โปรตีนไฮโดรไลเสตจากเมล็ดผลไม้ไทยเพื่อการบำบัดโรค : รายงานวิจัยฉบับสมบูรณ์ (ปีที่ 1) | en_US |
dc.type | Technical Report | en_US |
dc.email.author | Aphichart.K@Chula.ac.th | - |
Appears in Collections: | Biotec - Research Reports |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Apichart k_Res_.pdf | 542.51 kB | Adobe PDF | View/Open |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.