2008
DOI: 10.2478/v10035-008-0059-5
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ε-Aminocaproic Acid (EACA)

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Cited by 2 publications
(3 citation statements)
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“…It splits C-end amino-acids from peptides and proteins, especially quickly if phenyloalanine residue occurs in the penultimate position, in a weakly acidic environment [12,[19][20][21]. Our results are in accord with this.…”
Section: Resultssupporting
confidence: 86%
See 1 more Smart Citation
“…It splits C-end amino-acids from peptides and proteins, especially quickly if phenyloalanine residue occurs in the penultimate position, in a weakly acidic environment [12,[19][20][21]. Our results are in accord with this.…”
Section: Resultssupporting
confidence: 86%
“…Cathepsin A participates in protein degradation and activates/inactivates peptic hormones and biologically active peptides [20,22]. This enzyme has no endogenous inhibitors [23] and its peptidizing activity depends on the availability of the substrate, and a pH of between 4.5 and 5.5 [20,23]. In a pH of 7.0-7.5, cathepsin A shows amidazing and esterazing activity [22,24].…”
Section: Resultsmentioning
confidence: 99%
“…The terminal elimination half-life for AMI-CAR (aminocaproic acid) is $2 to 3 hours. 45 Because reports of basic, experimental, and in vitro studies 27,46,47 suggested that TXA is 7 to 10 times more potent than ε-ACA, 48,49 previous studies have used very high doses of aminocaproic acid (7-10 g) to try to equate the pharmacological effect of both drugs; however, the dose of ε-ACA that is the optimal equivalent to the TXA dose has not been established. Boese et al, 2017 use an equivalence of 7 g of ε-ACA with 1 g of TXA administered intravenously, found that there were no clinically significant differences regarding transfusion rates and blood loss in postoperated patients of a total knee arthroplasty.…”
Section: Discussionmentioning
confidence: 99%