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English to Swedish: Hemoglobin structure Detailed field: Chemistry; Chem Sci/Eng
Source text - English Hemoglobin is a complex molecule composed of two pairs of polypeptide chains. Each chain is linked to the heme, a tetrapyrrolic nucleus (porphyrin) which chelates an iron atom. The heme part is common to all hemoglobins and their variants. The type of hemoglobin is determined by the protein part called globin. Polypeptide chains a, b, d and g constitute the normal human hemoglobins:
• hemoglobin A = a 2 b 2
• hemoglobin A2 = a 2 d 2
• fetal hemoglobin F = a 2 g 2
The a-chain is common to these three hemoglobins.
The hemoglobin spatial structure and other molecular properties (as that of all proteins) depend on the nature and the sequence of the amino acids forming the chains. Substitution of amino acids by mutation is responsible for formation of hemoglobin variants which have different surface charge and consequently different electrophoretic mobilities, which also depend on the pH and ionic strength of the buffer.
The resulting qualitative (or structural) abnormalities are called hemoglobinopathies. Decreased synthesis of one of the hemoglobin chains leads to quantitative (or regulation) abnormalities, called thalassemias.
The assay is performed on the hemolyzate from washed red blood cells. The hemoglobins are separated by electrophoresis on alkaline gels and the fractions are visualized by staining with amidoblack. The dried gels are ready for interpretation
Translation - Swedish Hemoglobin är en komplex molekyl bestående av två par av polypeptidkedjor. Varje kedja är kopplad till hemet, en tetrapyrrolisk kärna (porfyrin) vilken kelaterar en järnatom. Hemdelen är gemensam för alla hemoglobiner och deras varianter. Typen av hemoglobin bestäms av proteindelen kallad globin. Polypeptidkedjorna a, b, d och g utgör de normala mänskliga hemoglobinerna:
• hemoglobin A = a 2 b 2
• hemoglobin A2 = a 2 d 2
• fetal hemoglobin F = a 2 g 2
a-kedjan är gemensam för dessa tre hemoglobiner.
Hemoglobinets spatiella struktur och andra molekylära egenskaper (som hos alla proteiner) beror på naturen och sekvensen av aminosyrorna som formar kedjorna. Utbyte av aminosyror genom mutationer har gett bildning av hemoglobinvarianter med annorlunda ytladdningar och således annan elektroforetisk rörlighet, vilket också beror på pH och jonstyrkan hos bufferten.
De resulterande kvalitativa (eller strukturella) abnormaliteterna kallas hemoglobinpatier. Minskad syntes hos en av hemoglobinkedjorna leder till kvantitativa (eller regulerings-) abnormaliteter, kallade thalassemier.
Metoden utförs på hemolysat från tvättade röda blodkroppar. Hemoglobinerna separeras genom elektrofores på alkaliska geler och fraktionerna visualiseras genom färgning med amidosvart. De torkade gelerna är redo för utvärdering.
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