69-25-0 Usage
General Description
Eledoisin is a small peptide composed of eleven amino acids that is found in the venom of the sea anemone Anemonia sulcata. It acts as a potent vasodilator, meaning it relaxes and widens blood vessels, leading to a decrease in blood pressure and an increase in blood flow to various tissues. Eledoisin also has the ability to induce smooth muscle contraction in the gastrointestinal tract and stimulate the secretion of gastric acid. Due to its physiological effects, eledoisin has been studied for its potential use in the treatment of conditions such as hypertension, gastric ulcers, and other circulatory disorders. Additionally, it has been used as a research tool to better understand the physiology and pharmacology of blood vessels and smooth muscle.
Check Digit Verification of cas no
The CAS Registry Mumber 69-25-0 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 6 and 9 respectively; the second part has 2 digits, 2 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 69-25:
(4*6)+(3*9)+(2*2)+(1*5)=60
60 % 10 = 0
So 69-25-0 is a valid CAS Registry Number.
InChI:InChI=1/C54H85N13O15S/c1-7-30(4)44(53(81)57-27-42(70)60-36(24-29(2)3)49(77)61-33(45(56)73)20-23-83-6)66-50(78)37(25-32-14-9-8-10-15-32)63-46(74)31(5)58-48(76)38(26-43(71)72)64-47(75)34(16-11-12-21-55)62-51(79)39(28-68)65-52(80)40-17-13-22-67(40)54(82)35-18-19-41(69)59-35/h8-10,14-15,29-31,33-40,44,68H,7,11-13,16-28,55H2,1-6H3,(H2,56,73)(H,57,81)(H,58,76)(H,59,69)(H,60,70)(H,61,77)(H,62,79)(H,63,74)(H,64,75)(H,65,80)(H,66,78)(H,71,72)/t30-,31-,33-,34-,35-,36-,37-,38-,39-,40-,44-/m0/s1
69-25-0Relevant articles and documents
Reaction medium engineering in enzymatic peptide fragment condensation: Synthesis of eledoisin and LH-RH
Bjoerup, Peter,Torres, Josep Lluis,Adlercreutz, Patrick,Clapes, Pere
, p. 891 - 901 (2007/10/03)
The influence of different reaction systems on α-chymotrypsin-catalyzed synthesis of eledoisin and LH-RH peptides from (7+4) and (5+5) fragments was investigated. The peptide yield was determined in the following systems: buffered aqueous media, frozen solutions, organic media, and cosolvent mixtures. The experimental set up was tailored to allow the screening of an array of conditions with minimum consumption of peptide fragments (2.1 and 2.5mM). The best yields (22% yield for eledoisin and 68% yield for LH-RH) were obtained in buffered aqueous solutions. It was found that the choice of buffer had a strong influence on the peptide yield; boric-borate and ammonium acetate buffers at pH 9, gave the best results. In buffered aqueous systems, both syntheses were scaled up by using a 10-fold increase in fragment concentration (21 and 25mM). Under these conditions the yields rose to 57% and 80% of eledoisin and LH-RH, respectively. Moreover, during the synthesis of eledoisin and in the presence of boric-borate buffer pH 9, the peptide precipitated from the reaction medium preventing a secondary hydrolysis and facilitating the in situ product purification. Copyright (C) 1998 Elsevier Science Ltd.
