It is required as supplement in cell culture media. Since the 1970s LMW heparin is used for surgery patients to avoid uncontrolled thrombosis (Linhardt and Gunay 1999).ДЄdditionally, since the 1970s heparin is also used in biotechnological processes. It shows the desired pharmacological effect, a better bioavailability, a higher therapeutic index, and fewer side effects. LMW heparin features defined biological and chemical properties. To avoid these side effects, a low-molecular-weight (LMW) heparin fraction was isolated. Nevertheless, studies at the Mayo Clinic, Minnesota, revealed that heparin causes side effects such as headaches, fever, nausea, or heparin-induced thrombocytopenia (HIT) (Best 1959). In 1959, Crafoord and Best showed that heparin treatment prevents postoperative thrombosis. At the same time, Jorpes in collaboration with Charles and Scott prepared heparin with acceptable purity for human trials. Several research groups expanded the isolation of heparin first from bovine lung and later from porcine intestine (Liu et al. Furthermore, he found out that the sulfo groups are located at the N-residue of GlcN. Jorpes determined in 1936 that heparin contains a high amount of sulfo groups which makes heparin one of the strongest known acids. Seven years later in 1935, Bergstrom and Jorpes discovered glucosamine (GlcN) as the second sugar component in heparin (Jorpes and BergstrГ¶m 1936). In 1928, Howell identified uronic acid as one sugar component in heparin. It was called heparin (Greek hepar-liver) (McLean 1959 Marcum 1997). The discovery of heparin took place in 1916 when Jay McLean and William Howell isolated a glycosaminoglycan from liver tissues that inhibited blood coagulation. Moreover, the usage of other chromatographic systems mimetic the heparin effect is reviewed.

Thereby, alternatives for the provision of heparin such as chemical synthesized heparin, chemoenzymatic heparin, and bioengineered heparin are discussed. This review examines strategies to avoid these disadvantages. Hence, adequate alternatives to animal-derived components are needed. Therefore, they are liable to strict quality controls and the validation of effective good manufacturing practice (GMP) implementation. Animal-based components carry the risk of contamination. While effective, it is disadvantageous that heparin is an animal-derived material. Diverse recombinant proteins can be successfully purified by this method. This review focuses on the heparin affinity chromatography.

An understanding of the heparin-protein interactions at the molecular level is not only advantageous in the therapeutic application but also in biotechnological application of heparin for downstreaming. This review gives a general overview of specific patterns and functional groups which are involved in the heparin-protein binding. To date, the structural heparin-protein interactions are not completely understood. HeparinвЂ™s activities are associated with its interaction to various proteins. These properties are employed in several therapeutic drugs. The major biological purpose is the inhibition of the coagulation cascade to maintain the blood flow in the vasculature. It is involved in various important biological activities. Heparin is a highly sulfated polysaccharide which belongs to the family of glycosaminoglycans.

Capto mmc pi cation interaction