Chapter-10 Hemoglobin Metabolism Flashcards
the most studied proteins in the body due to the ability to easily isolate it from red blood cells (RBCs)
Hemoglobin
the concentration of hemoglobin within RBCs
approximately 34 g/dl,
Hemoglobins main function
Is to transport oxygen from the tissues and transport carbon dioxide from the tissues to the lungs for exhalation.
heme consist of a ring of carbon, hydrogen, and nitrogen atoms called
protoporphyrin IX, carries a central ferrous Ion (Fe+2)
oxidized hemoglobin is also called
Methemoglobin
Alpha
141 #of amino acid
beta
146
gamma A
146 (position 136:alanine)
Gamma G
146 (position: glycine)
Delta
146
Epsilon
146
Zeta
141
Theta
unknown
refers to the amino acid sequence of the polypeptide chains
Primary structure
refers to chain arrangements in helices and non helices
secondary structure
refers to the arrangements of the helices into a pretzel-like configuration.
tertiary structure
The predominant adult hemoglobin
Hb A, composed of two a-globin chains and
two b-globin chains. Strong a1–b1 and a2–b2 bonds hold the
dimers in a stable form. The a1–b2 and a2–b1 bonds are important for the stability of the quaternary structure in the oxygenated and deoxygenated forms
Occurs in the mitochondria and cytoplasm
of bone marrow erythrocyte precursors, beginning with the
pronormoblast through the circulating polychromatic (also
known as polychromatophilic) erythrocyte
Heme biosynthesis
it is where the production of globin chains takes place
erythroid precursors
