Hemoglobin produced in association with the sickle cell trait; the beta-globin molecules of hemoglobin S are defective.
The difference in electrophoretic pattern between normal hemoglobin A and hemoglobin S is due to a single amino acid substitution. In hemoglobin S, a glutamic acid is replaced by a valine at position 6 of the beta-globin chain. This change causes hemoglobin S to have a different charge, leading to its characteristic migration pattern on electrophoresis.
hemoglobin is what give the red blood cells it,s clour
glutamic acid is replaced by valine in the beta chain
4 months
Hemoglobin S refers to the hemoglobin that forms in patients with sickle cell anemia. Hemoglobin solubility is a test that can be performed in order to determine if the patient has sickle cell anemia.
H. Lehmann has written: 'Human haemoglobin variants and their characteristics' -- subject(s): Hemoglobin, Tables 'Man's haemoglobins' -- subject(s): Hemoglobin, Hemoglobinopathy
Hemoglobin electrophoresis uses stains such as Coomassie blue or Ponceau S to visualize the globin chains of the hemoglobin molecule. These stains help separate and identify different types of hemoglobin based on the migration pattern of the globin chains.
Do hemoglogin electrophoresis
A hemoglobin is a red protein responsible for transporting oxygen in the blood of vertebrates. Its molecule comprises four subunits, each containing an iron atom bound to a heme group. TO answer your question. THe answer is a big, fat "NO".
hemoglobin
Robert M. Winslow has written: 'Advances in Blood Substitutes' 'Hemoglobin-based red cell substitutes' -- subject(s): Blood Substitutes, Hemoglobin
No, hemoglobin is a protein.