MS 워드 
소개글
hematology, hemoglobin, hematoglobinophathy, hemolysis, heinzbody 등 헤모글로빈에 대한 영어 레포트 입니다.목차
Haemoglobin (Hb)Hematoglobinopathy
Intravascular and extravascular hemolysis
Clinical features
Laboratory feature
References
본문내용
Haemoglobin is a conjugated protein and composed of four subunits, two α and two β which entail four hemes in which protoporphyrin IX is positioned with ferrous iron(Fe^(2+)). The heme group is where oxygen binding occurs. O2 molecules bind to protein molecule with covalent bond to Fe^(2+). Heme contains four pyrrole groups that interact covalent bonds with four of iron positions. Covalent bond is formed in one position, creating a chain of histidine amino acid, which is called the proximal histidine. Oxygen molecue converts Fe^(2+) to Fe^(3+) in heme molecue. The presence of the distal histidin can prevent oxidation of the heme by formation of Fe-O-O bond (1). It also allows passage of oxygen out or into the haemoglobin. Amino acids outside the cleft are hydrophilic while amino acids inside the cleft are hydrophobic. In this formation, divalent ferrous form of iron can remain. Hemoglobin molecule has four heme groups that may carry four oxygen molecules (2,3).참고 자료
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