Heparinic acid

Masamune, Suzuki and Kondoh were the first to suggest a sulfuric group in heparin in the form of bridges, —C—O—SO2—NH—C—, but they presented no experimental evidence therefor. This suggestion was criticized by Jorpes, Bostrom and Mutt, who pointed out that Wilander " had shown that all the sulfate groups in heparin (acid form) are free and... 

The presence of low molecular weight substances of unknown nature About 20 per cent by weight of heparin can be removed by prolonged dialysis of the heparinic acid . 

CAS 9005-49-6 EINECS/ELINCS 232-681-7 Synonyms a-Heparin Heparinate Heparinic acid Heparin sulfate Vitamin AB... 

Heparinate Heparinic acid. See Heparin Heparin lithium... 

CAS 9045-22-1 EINECS/ELINCS 232-681-7 Definition Lithium salt of heparinic acid Properties Wh. powd. sol. in water Uses Anticoagulant in medical devices laboratory reagent Manuf/Distrib. CarboMer http //www.carbomer.com] Fluka http //www.sigma-aidrich.com] Sigma Trade Name Synonyms SPL Heparin Lithium [Scientific Protein Labs http //www.spi-pharma.com]... 

The sodium salts of sulphuric acid esters of dextran are used as anticoagulants for the same purposes as heparin. 

Substances other than enzymes can be immobilized. Examples include the fixing of heparin on polytetrafluoroethylene with the aid of PEI (424), the controUed release of pesticides which are bound to PEI (425), and the inhibition of herbicide suspensions by addition of PEI (426). The uptake of anionic dyes by fabric or paper is improved if the paper is first catonized with PEI (427). In addition, PEI is able to absorb odorizing substances such as fatty acids and aldehydes. Because of its high molecular weight, PEI can be used in cosmetics and body care products, as weU as in industrial elimination of odors, such as the improvement of ambient air quaHty in sewage treatment plants (428). 

In contrast to heparin, the coumarinic acid anticoagulants are inactive in vitw ]6k.e heparin they are active in vivo. The phenylindanedione-type compounds (7) (36) and warfarin (2) produce their in vivo inhibitory effect on the coagulation system by competitively antagonizing the normal activity of vitamin (8) (37—44). 

There are other glycosaminoglycans. Hyaluronic acid [9004-61-9] occurs both free and in noncovalent association with proteoglycan molecules. Heparin [9005-49-6] and heparan sulfate [39403-40-2] also known as heparitin sulfate [9050-30-0] occur in mast cells and in the aorta, Hver, and lungs. 

Prourokinase is a single-chain protein containing 411 amino acids (261,265,274,275). In clinical uses scu-PA does not bind to fibrin only and its use causes a decreased plasma fibrinogen of 80%. Its half-life in the circulation is 5 min. It is cleared by the fiver. It is used at 40—70 mg over 1 h and heparin is needed simultaneously. Fibrin specificity and thrombolytic efficacy are similar to that of t-PA. 

Heparin inhibits the formation of fibrin clots, inhibits the conversion of fibrinogen to fibrin, and inactivates several of the factors necessary for the clotting of blood. Heparin cannot be taken orally because it is inactivated by gastric acid in the stomach therefore, it must be given by injection. Heparin has no effect on clots that have already formed and aids only in preventing the formation of new blood clots (thrombi). The LMWHs act to inhibit clotting reactions by binding to antithrombin HI, which inhibits the synthesis of factor Xa and the formation of thrombin. 

The theory and application of this fluorescence method have been discussed in detail by LePecq and others (3,8). The assay requires that there is sufficient ionic strength to minimize ionic binding (e.g., O.IM sodium chloride), that the pH is 4-10, that no heavy metals are present, that the fluorescence is not enhanced on binding to other excipients (e.g., proteins) and that at least portions of the nucleic acids are not complexed. These requirements can usually he met when dealing with recombinant products in some cases the samples must he manipulated to create the appropriate conditions. In the intercalative method of dye binding, proteins rarely interfere with the assay, and procedures have been developed to remove the few interferences they may cause (e.g., the use of heparin or enzymatic digestion of the protein 9). 

A typical procedure is shown in Figure 2. Other dyes besides ethidium can be used, although ethidium has an advantage in that its excitation emission bands are well removed from any protein absorbances. A standard curve can be constructed for the nucleic acid of concern and the limits of detection established. In Step 3, proteolytic enzymes may be substituted for heparin, or the step may be bypassed in the case of proteins which do not interfere. After measurement of the unknown sample the nucleic acid concentration may be simply calculated or read from the standard curve. 

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