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PubMed1984

Inhibition of the activation of the first component of complement, C1, by various amino acids or peptides.

The effects of various amino acids (or their analogues) and peptides on the activation or consumption of human complement by erythrocytes bound with hemolysin or heat-aggregated immunoglobulin G (aggIgG) were studied by using the hemolysis of hemolysin-bound erythrocytes, the consumption of complement by aggIgG in the serum, the hydrolysis of acetyl tyrosine ethyl ester by activated Cl (Cls), Cl hemolysis and a newly developed enzyme immunoassay, which directly measures interaction between Clq and aggIgG. Amino acids or peptides which were proposed to comprise Clq binding sites of the C2 region of IgG or their analogues were used. CH50 was inhibited by lysine or arginine to the largest extent, but other amino acids, including tranexamic acid and epsilon-amino caproic acid were not inhibitory up to 60 mM. The consumption of serum complement by aggIgG was prevented by arginine or lysine (about 60% inhibition at 60 mM) and by histidine to a lesser extent. The activation of Cls in the Cl complex by aggIgG precipitated at pH 5.5 was most inhibited by lysine, and to a lesser extent by tranexamic acid, arginine and epsilon-aminocaproic acid, but not glutamic acid or glycine. The results of Cl hemolysis indicated that, of all amino acids soluble at neutral pH, lysine and arginine were most effective in the inhibition of Cl hemolysis. Tranexamic acid and epsilon-aminocaproic acid were less effective, and glycine and norleucine were hardly effective. Among the dipeptides used, those that are composed of aromatic amino acids were very effective in the inhibition of Cl hemolysis.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗

PubMed2003

Pharmacological approaches to reducing allogeneic blood exposure.

This article discusses evidence for the role of pharmacological interventions such as the protease inhibitor aprotinin (Trasylol), lysine analogue anti-fibrinolytics [tranexamic acid (Cyclokapron) and epsilon aminocaproic acid (Amicar)], DDAVP (Desmopressin) and recombinant Factor VIIa (NovoSeven), in preventing the need for blood and blood-component therapies after major (cardiac, hepatic and orthopaedic/trauma) surgery. The data show that aprotinin is consistently effective in reducing globally the transfusion burden in cardiac and hepatic surgical procedures. However, there are little data to support its use in routine elective orthopaedic surgery. Multiple studies have failed to show an increased risk for myocardial ischaemia or infarction with aprotinin, and there may even be a reduced incidence of perioperative stroke in patients undergoing cardiac surgery. An increased probability of a hypersensitivity reaction when the drug is readministered within a 6-month period remains a significant issue. The data for the lysine analogue anti-fibrinolytics show no evidence of efficacy in reducing the transfusion burden for epsilon aminocaproic acid and inconsistent results with tranexamic acid in cardiac and hepatic surgery. As with aprotinin therapy, there is a paucity of data to support their use in routine elective orthopaedic surgery. There are no data to support the routine use of DDAVP to reduce the transfusion burden. Limited data suggest that this drug may be effective when a defect in platelet function is demonstrated. This aspect deserves further investigation. Recombinant activated Factor VII (rFVIIa) has proven benefit for its licensed indication to reduce bleeding in haemophiliacs with inhibitors to Factors VIII and IX. Reports of benefit in other instances are largely anecdotal. Hence, at this time it is therefore speculative and premature to suggest whether there is a place for this agent in routine clinical practice. No adequately powered, placebo-controlled prospective studies are available to investigate the safety of the lysine analogues, DDAVP or rFVIIa in cardiac, hepatic or orthopaedic surgery.

Blood Loss, Surgical↗

PubMed1990

Purification of carnitine palmitoyltransferase from heart mitochondria by hydrophobic affinity chromatography.

Carnitine palmitoyltransferase II of rat heart mitochondria was purified to homogeneity by a rapid method exploiting the hydrophobic nature of the protein. The method involves solubilization of mitochondrial membrane proteins by detergents and subsequent fractionation by hydrophobic affinity chromatography. Sepharose, cross-linked via a primary amino group of 1,omega-diaminoalkane, 4-aminobutyric acid, 6-aminocaproic acid, or 6-aminohexanol, was found to reversibly bind carnitine palmitoyltransferase under nondenaturing conditions. A homologous series of n-alkyl-agarose resins with n = 2 to 8 and phenyl-Sepharose were also found to reversibly bind the enzyme. Alkyl-Superose, phenyl-Superose, and Superose 12 chromatographies were also very useful in fractionating the enzyme. Successive chromatography on three or four hydrophobic columns yielded a highly pure enzyme preparation. The purified preparation appeared as one major protein band on polyacrylamide electrophoresis gels in the presence of sodium dodecyl sulfate (M(r) 68,000). The isolated enzyme had significant activity (sp act = 15.0 mumol/min/mg protein when 80 microM palmitoyl-CoA and 20 mM carnitine were used as substrates). Antibodies against this protein recognized (in immunoblots) one major protein band in crude preparations of rat heart mitochondria (M(r) 68,000), indistinguishable from purified carnitine palmitoyltransferase II. L-Palmitoylcarnitine (0.1 mM) and coenzyme A (0.1 mM), products of the enzyme-catalyzed reaction, inhibited carnitine palmitoyltransferase activity 66 and 71%, respectively. D-Palmitoylcarnitine (0.1 mM), however, did not inhibit the activity. Malonyl-CoA, a specific inhibitor of membrane-bound carnitine palmitoyltransferase I, did not show significant inhibition.

Animals↗

PubMed1997

Fibrinolytic inhibitors for cancer-associated bleeding problems.

This pilot study of 16 patients explored the use of two fibrinolytic inhibitors, tranexamic acid and aminocaproic acid, for the suppression of tumor-associated hemorrhage. The effects of such bleeding include anemia requiring transfusion, practical difficulties with dressings, and psychological morbidity from constant reminder of poor physical health. Cessation of bleeding occurred in 14 of the 16 patients treated. The average time until significant improvement in bleeding was just 2 days and the average time for complete cessation was 4 days. We conclude that fibrinolytic inhibitors are potentially useful agents in palliative care.

Adult↗

PubMed1976

Inhibition of the development of the cellular slime mould Dictyostelium discoideum by omega-aminocarboxylic acids.

Four omega-aminocarboxylic acids - epsilon-aminocaproic acid (EACA), trans-4-aminomethylcyclohexane-1-carboxylic acid (t-AMCHA), p-aminomethylbenzoic acid (PAMBA) and omega-aminocaprylic acid (OACA) -- prevented fruiting body formation of the cellular slime mould Dictyostelium discoideum. At concentrations of 40 mM, 75 mM, 10 mM and 5 mM, respectively, they allowed aggregation but prevented all further development at 24 degrees C. At lower concentrations, EACA allowed fruiting body formation but with a reduced number of spores per fruiting body. Only t-AMCHA had a significant inhibitory effect on the growth of myxamoebae. EACA affected development only if it was present between 8 and 16 h after the cells were deposited on the filters. Its effect was enhanced by high salt concentrations and by higher temperature, and was also dependent on the manner in which the cells were grown. Only strains capable of axenic growth displayed this sensitivity to EACA, although strains carrying only one of the genetic markers for axenic growth (axe A) were partially sensitive.

4-Aminobenzoic Acid↗

PubMed2006

Hemostatic mouthwashes in anticoagulated patients undergoing dental extraction.

OBJECTIVE: To evaluate the efficacy and safety of local acting hemostatic agents in patients who are undergoing dental extraction(s) and are taking oral anticoagulants. DATA SOURCES: A search of MEDLINE (1966-July 2006), International Pharmaceutical Abstracts (1970-July 2006), and EMBASE (1966-July 2006) was conducted using the key terms anticoagulation, warfarin, hemostatic mouthwashes, epsilon aminocaproic acid, tranexamic acid, dental extraction, and oral surgery. Bibliographies of relevant papers were reviewed for additional references. STUDY SELECTION AND DATA EXTRACTION: English-language literature, including abstracts, clinical trials, and review articles, were reviewed. Clinical trials were included if they evaluated hemostatic mouthwashes in patients receiving continued anticoagulation and undergoing dental extractions or various oral surgeries including dental extraction. Eight clinical trials met study selection criteria for evaluation of hemostatic mouthwashes in anticoagulated patients undergoing dental extraction. Eight studies evaluated tranexamic acid; one assessed epsilon aminocaproic acid. All studies were reviewed for efficacy and safety of hemostatic mouthwashes and intensity of continued anticoagulation therapy. DATA SYNTHESIS: Eight small studies enrolled populations that varied in the indications for oral anticoagulation (OA), target INR ranges, and oral surgeries performed. Patients receiving uninterrupted OA and using hemostatic mouthwashes had no greater and, in some cases, lesser bleeding incidence compared with various other treatment groups (including interrupted OA, uninterrupted OA, autologous fibrin glue with uninterrupted OA, and reduced OA with heparin bridge). No severe adverse effects were reported. No studies assessed the risk of thromboembolism between the different treatment strategies. CONCLUSIONS: Findings in recent studies indicate that dental extractions in anticoagulated patients can be performed without temporary discontinuation of oral anticoagulant therapy with the use of hemostatic mouthwashes to control localized bleeding. This practice should be more widely adopted due to minimized bleeding and thromboembolic risks.

Anticoagulants↗

PubMed2004

Management of bleeding in patients with advanced cancer.

Bleeding occurs in up to 10% of patients with advanced cancer. It can present in many different ways. This article provides a qualitative review of treatment options available to manage visible bleeding. Local modalities, such as hemostatic agents and dressings, radiotherapy, endoscopic ligation and coagulation, and transcutaneous arterial embolization, are reviewed in the context of advanced cancer, as are systemic treatments such as vitamin K, vasopressin/desmopressin, octreotide/somatostatin, antifibrinolytic agents (tranexamic acid and aminocaproic acid), and blood products. Considerations at the end of life are described.

Antifibrinolytic Agents↗

PubMed2002

Pharmacological strategies to decrease transfusion requirements in patients undergoing surgery.

Surgical procedures are inevitably associated with bleeding. The amount of blood loss may vary widely between different surgical procedures and depends on surgical as well as non-surgical factors. Whereas adequate surgical haemostasis may suffice in most patients, pro-haemostatic pharmacological agents may be of additional benefit in patients with (diffuse) surgical bleeding or in patients with a specific underlying haemostatic defect. In general, surgical haemostasis and pharmacological therapies can be complementary in controlling blood loss. The use of pharmacological therapies to reduce blood loss and blood transfusions in surgery has historically been restricted to a few drugs. Antifibrinolytic agents (aprotinin, tranexamic acid and aminocaproic acid) have the best evidence supporting their use, especially in cardiac surgery, liver transplantation and some orthopaedic surgical procedures. Meta-analyses of randomised, controlled trials in cardiac patients have suggested a slight benefit of aprotinin, compared with the other antifibrinolytics. Desmopressin is the treatment of choice in patients with mild haemophilia A and von Willebrand disease. It has also been shown to be effective in patients undergoing cardiac surgery who received aspirin up to the time of operation. However, overall evidence does not support a beneficial effect of desmopressin in patients without pre-existing coagulopathy undergoing elective surgical procedures. Topical agents, such as fibrin sealants have been successfully used in a variety of surgical procedures. However, only very few controlled clinical trials have been performed and scientific evidence supporting their use is still limited. Novel drugs, like recombinant factor VIIa (eptacog alfa), are currently under clinical investigation. Recombinant factor VIIa has been introduced for the treatment of haemophilia patients with inhibitors, either in surgical or non-surgical situations. Preliminary data indicate that it may also be effective in surgical patients without pre-existing coagulation abnormalities. More clinical trials are warranted before definitive conclusions can be drawn about the safety and the exact role of this new drug in surgical patients. Only adequately powered and properly designed randomised, clinical trials will allow us to define the most effective and the safest pharmacological therapies for reducing blood loss and transfusion requirements in surgical patients. Future trials should also consider cost-effectiveness because of considerable differences in the costs of the available pro-haemostatic pharmacological agents.

Administration, Topical↗

PubMed2001

Transfusion medicine : support of patients undergoing cardiac surgery.

There is still no alternative that is as effective or as well tolerated as blood; nevertheless, the search for ways to conserve, and even eliminate blood transfusion, continues. Based on hemoglobin levels, practice guidelines for the use of perioperative transfusion of red blood cells in patients undergoing coronary artery bypass grafting have been formulated by the National Institutes of Health and the American Society of Anesthesiologists. However, it has been argued that more physiologic indicators of adequacy of oxygen delivery should be used to assess the need for blood transfusion. Methods used for conserving blood during surgery include autologous blood donation, acute normovolemic hemodilution and intra- and postoperative blood recovery and reinfusion. The guidelines for the use of autologous blood transfusion are controversial and it does not appear to be cost effective compared with allogeneic blood transfusion in patients undergoing cardiac surgery. Similarly, the cost effectiveness of intra- and postoperative blood recovery and reinfusion need further evaluation. Treatment with recombinant human erythropoietin (rhEPO) remains unapproved in the US for patients undergoing cardiac or vascular surgery, but it is a valuable adjunct in Jehovah's Witness patients, for whom blood is unacceptable. The characterization of darbepoetin alfa, a novel erythropoiesis stimulating protein with a 3-fold greater plasma elimination half-life compared with rhEPO, is an important advance in this field. Darbepoetin alfa appears to be effective in treating the anemia in patients with renal failure or cancer and trials in patients with surgical anemia are planned. Desmopressin has been used to effectively reduce intraoperative blood loss. Topical agents to prevent blood loss, such as fibrin glue and fibrin gel, and agents that alter platelet function, such as aspirin (acetylsalicylic acid) or dipyridamole, need further evaluation in patients undergoing cardiac surgery. Aprotinin has been shown to preserve hemostasis and reduce allogeneic blood exposure to a greater extent than the antifibrinolytic agents tranexamic acid and aminocaproic acid. Controlled clinical trials comparing the costs of these agents with clinical outcomes, along with tolerability profiles in patients at risk for substantial perioperative bleeding are needed.

Blood Loss, Surgical↗

PubMed1977

Cutaneous vascular fibrinolytic activity in the local Shwartzman reaction.

A fibrin slide test was utilized to study cutaneous vascular plasminogen activator activity in normal rabbit, rat, monkey, and human skin and in rabbit skin following development of the local Shwartzman reaction and after substituting epsilon-aminocaproic acid for the preparatory injection of endotoxin in the local Shwartzman reaction. Cutaneous vascular plasminogen activator activity was also studied in rats after attempted induction of the local Shwartzman reaction following inhibition of fibrinolysis with epsilon-aminocaproic acid and/or pregnancy. Plasminogen activator activity was detected in vessels of normal rat, monkey, and human skin but was absent in skin from normal rabbits and rabbits with the local Shwartzman reaction. Intradermal injection of epsilon-aminocaproic acid failed to prepare for the local Shwartzman reaction. In the rat, which has greater cutaneous vascular plasminogen activator activity than the rabbit, inhibition of vascular activator with epsilon-aminocaproic acid and/or pregnancy failed to prepare for the local Shwartzman reaction. These studies indicate that although the markedly diminished level of cutaneous vascular plasminogen activator in the rabbit may be important in the pathogenesis of the local Shwatzman reaction, factors other than inhibition of fibrinolysis are also necessary for preparation of the reaction.

Aminocaproic Acid↗

PubMed1975

The importance of the preactivation peptide in the two-stage mechanism of human plasminogen activation.

The two stages in the activation of human plasminogen by urokinase have been examined kinetically in order to evaluate the significance of each stage in the activation process. The cleavage of the preactivation peptide from the NH2 terminus of native plasminogen (NH2-terminal glutamic acid) is clearly catalyzed by urokinase and is the rate-limiting first step in activation (Stage 1); this reaction is 20-fold slower than the conversion of the intermediate plasminogen (NH2-terminal lysine) to plasmin (Stage 2). Both lysine and its analogoue, epsilon-aminocaproic acid, exert two effects on the activation of native plasminogen. At low concentrations of these agents, activation is greatly accelerated. Analysis of activation in the presence and absence of these agents by sodium dodecyl sulfate gel electrophoresis indicates that the activation pathway is the same in both cases with the formation of a transient intermediate plasminogen; only the kinetics of proteolysis are altered. This enhancement in the rate of activation results solely from acceleration of the Stage 1 reaction; Stage 2 is essentially unaffected at low concentrations. Stage 1 is maximally enhanced (75-fold) at either 0.0025 M epsilon-aminocaproic acid or 0.025 M lysine and occurs 4 times more rapidly than Stage 2, which becomes the rate-limiting step at these concentrations. Plasmin also cleaves the preactivation peptide from native plasminogen and this reaction rate is enhanced by the same concentrations of lysine and epsilon-aminocaproic acid. These data suggest that lysine and epsilon-aminocaproic acid, which are known to bind to plasminogen and significantly alter its conformation, may thereby enhance preactivation peptide cleavage and consequently, plasminogen activation. At high concentrations, both Stages 1 and 2 are similarly inhibited by these agents, which suggests that this effect may be exerted by the direct inhibition of urokinase. The relative rates of preactivation peptide cleavage by the enzymes urokinase, plasmin, thrombin, and ancrod were also determined. Urokinase is 10 times more effective than plasmin in catalyzing this reaction and 1.8 X 10(4) times more effective than thrombin, while ancrod does not exert an effect. No plasmin is formed by either thrombin or ancrod.

Amino Acid Sequence↗

PubMed1983

The role of the lysine binding sites of human plasmin in the hydrolysis of human fibrinogen.

The importance of the lysine binding sites of human plasmin for its ability to digest human fibrinogen has been assessed by analyzing the nature and rate of the products formed in the presence of epsilon-aminocaproic acid. No major differences in this regard were found when comparing Lys77-plasmin and Val442-plasmin, in the absence of epsilon-aminocaproic acid, the latter plasmin being devoid of the lysine binding sites present on residues Glu1-Val441 (K 1-4). The presence of epsilon-aminocaproic acid, at concentrations ranging from 0.5-5.0 mM, results in progressively stronger inhibition of the digestion of fibrinogen and in appearance of fibrinogen degradation products Y, D and E, for both Lys77-plasmin, and Val442-plasmin, showing the importance of lysine binding regions in this property. However, since both plasmin forms were inhibited equally well at all levels of epsilon-aminocaproic acid, these studies show that lysine binding sites other than those present on region K 1-4 of Lys77-plasmin are of primary importance to fibrinogenolysis by plasmin.

Binding Sites↗

PubMed2006

Efficacy of FDA-approved hemostatic drugs to improve survival and reduce bleeding in rat models of uncontrolled hemorrhage.

Several FDA-approved intravenous drugs are used to reduce surgical bleeding. This series of studies tested whether these drugs (aprotinin, desmopressin, tranexamic acid, epsilon-aminocaproic acid) could reduce bleeding due to traumatic injuries in two models of uncontrolled hemorrhage in rats. In the first phase of each study, a nonlethal tail bleeding model was used that incorporated limited fluid resuscitation (lactate Ringer's solution). Four doses of vehicle or the test substance were given successively with bleeding time and blood loss measured after each dose. In the second phase of each study, a lethal liver injury was produced by excising a section of the median lobe (approximately 0.8% of body weight) and an infusion of either vehicle or the test substance was immediately begun. This model included aggressive fluid resuscitation and a severe dilutional coagulopathy. Blood loss, survival time and mortality rate were recorded. Three studies were performed, testing each of the drugs singly and in combination. None of the drugs significantly reduced either bleeding time or blood loss in the tail bleeding model, nor were blood loss, survival time or mortality rate altered in the liver injury model. Taken together, these results suggest that these FDA-approved drugs, when used either singly or in combination, are not efficacious in these models of traumatic uncontrolled hemorrhage.

Aminocaproic Acid↗

PubMed1979

Studies on the mechanism of action of cetraxate [4'-(2-carboxyethyl)phenyl trans-4-aminomethyl cyclohexanecarboxylate hydrochloride], a new anti-ulcer agent.

To elucidate mechanisms involved in the anti-ulcer action of cetraxate, the effects of this agent on the ulcer index (UI), fibrinolytic activity (FA) and contents of several connective tissue components in ulcer tissue were examined using aspirin- and acetic acid ulcers in rats. In aspirin ulcer, cetraxate (100 and 300 mg/kg p.o.), like tranexamic acid (500 mg/kg p.o.), epsilon-aminocaproic acid (500 mg/kg p.o.) and gefarnate (200 mg/kg p.o.), inhibited both the UI and FA. However, aluminum sucrose sulfate (1000 mg/kg p.o.) was effective only against the UI and L-glutamine (500 mg/kg p.o.) failed to inhibit both parameters. In acetic acid ulcer, following oral, daily X either 5 or 8 administrations, cetraxate (200 and 300 mg/kg), gefarnate (200 mg/kg), aluminum sucrose sulfate (1000 mg/kg) and L-glutamine (500 mg/kg) were effective on both the UI and FA. Tranexamic acid (500 mg/kg) and epsilon-aminocaproic acid (500 mg/kg) were ineffective on the UI, although both agents inhibited FA. In acetic acid ulcer, cetraxate induced increases in hexosamine and uronic acid, that is, acid mucopolysaccharides (AMPS), especially chondroitin sulfate A and -C, whereas L-glutamine and aluminum sucrose sulfate resulted in increases in hexosamine and sialic acid, that is, glycoproteins. From these results, cetraxate may mainly accelerate the ulcer healing by increasing AMPS in ulcer tissue. Moreover, the local anti-FA property of this agent may be also beneficial in treating bleeding ulcers.

Acetates↗

PubMed1990

New ligands for human C-reactive protein: calcium-dependent binding with epsilon-aminocaproic acid-agarose and calcium-independent binding with omega-aminohexyl-agarose.

Human C-reactive protein (CRP) is an acute phase protein which increases in concentration in response to inflammation. CRP has been known to bind with phosphorylcholine in a calcium-dependent manner. In this study, CRP is found to bind to affinity chromatography of negatively-charged epsilon-aminocaproic acid-agarose when calcium ions are present, and to the affinity chromatography of positively-charged omega-aminohexyl-agarose if a normal ionic strength of NaCl exists but calcium ion is not present.

Aminocaproates↗

PubMed2003

Determination of egg white lysozyme by on-line coupled capillary isotachophoresis with capillary zone electrophoresis.

An on-line coupled capillary isotachophoresis - capillary zone electrophoresis method for the determination of lysozyme in selected food products is described. The optimized electrolyte system consisted of 10 mM NH(4)OH + 20 mM acetic acid (leading electrolyte), 5 mM epsilon -aminocaproic acid +5 mM acetic acid (terminating electrolyte), and 20 mM epsilon -aminocaproic acid +5 mM acetic acid +0.1% m/v hydroxypropylmethylcellulose (background electrolyte). A clear separation of lysozyme from other components of acidic sample extract was achieved within 15 min. Method characteristics, i.e., linearity (0-50 micrograms/mL), accuracy (recovery 96+/-5%), intra-assay (3.8%), quantification limit (1 microgram/ml), and detection limit (0.25 microgram/mL) were determined. Low laboriousness, sufficient sensitivity and low running costs are important attributes of this method. The developed method is suitable for the quantification of the egg content in egg pasta.

Calibration↗

PubMed1984

Kinetic and thermodynamic parameters for Schiff base formation of vitamin B6 derivatives with amino acids.

Thermodynamic and kinetic parameters for Schiff base formation of pyridoxal 5'-phosphate and pyridoxal with epsilon-aminocaproic acid as well as of pyridoxal 5'-phosphate with L-serine were obtained in 0.1 M sodium pyrophosphate buffer as a function of temperature. Changes in enthalpy, which were determined by direct microcalorimetry, were small at 25 degrees C, but varied strongly with pH for the reaction of pyridoxal 5'-phosphate with the amino acids. In contrast to the fast Schiff base formation of pyridoxal 5'-phosphate, a very slow reaction was found for pyridoxal and epsilon-aminocaproic acid concomitant with a larger change in enthalpy. By preventing hemiacetal formation the phosphate moiety plays a crucial role.

Amino Acids↗

PubMed1982

[Pharmacokinetic studies with 3H-labelled synthetic antifibrinolytics].

In rabbits and rats pharmacokinetic studies on the anti-fibrinolytics 4-aminomethylbenzoic acid (PAMBA), trans-4-aminomethylcyclohexane-1-carboxylic acid (AMCA), and epsilon-aminocaproic acid (EACA) were carried out using the tritium labelled compounds. Following i. v. administration of PAMBA and EACA in rabbits a two-phasic plasma level and following AMCA a three-phasic plasma level was found within 7 h. The rate constants beta of 0.34 h-1, 0.44 h-1, and 1.08 h-1 for EACA, PAMBA, and AMCA, respectively, indicate a more rapid elimination of AMCA. Accordingly, the AUC-values for AMCA are considerably smaller than those for EACA and PAMBA after both i. v. and p. o. administration.

4-Aminobenzoic Acid↗