By John W. Pelley PhD
Effectively merge uncomplicated technology and medical talents with Elsevier's built-in overview Biochemistry, by means of John W. Pelley, PhD. This concise, high-yield name within the renowned built-in evaluation sequence makes a speciality of the center wisdom in biochemistry whereas linking that details to similar options from different easy technology disciplines. Case-based questions on the finish of every bankruptcy help you gauge your mastery of the fabric, and a color-coded layout enables you to fast locate the categorical suggestions you would like. on-line entry through www.studentconsult.com - incorporated together with your buy - permits you to comfortably entry the book's entire textual content and illustrations on-line in addition to appropriate content material from different scholar seek advice titles. This concise and effortless reference offers an important suggestions for the early years of clinical education and USMLE preparation.
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Extra resources for Elsevier's Integrated Review Biochemistry: With STUDENT CONSULT Online Access, 2e
Fetal Hemoglobin 2,3-BPG has weaker binding to fetal hemoglobin (HbF) than to adult hemoglobin (HbA) because of the different amino acid composition at the allosteric site. This reduces the negative allosteric effect of 2,3-BPG, leading to a small increase in O2 affinity of HbF relative to HbA. This is a molecular adaptation to the low PO2 of the placental circulation; O2 flows from HbA (maternal circulation, lower O2 affinity) to HbF (fetal circulation, higher O2 affinity). Hemoglobinopathies Hemoglobinopathies are genetic diseases caused by structural alterations in the globin chains or by altered rates of globin synthesis.
Hemoglobin F, composed of a and g chains, is the predominant form in the fetus. Hemoglobin A, composed of a and b chains, is the predominant form in adults. One form of hemoglobin, hemoglobin A1C (HbA1C), is not determined genetically. It is a subclass of hemoglobin A that is formed from a spontaneous reaction between blood glucose and the amino terminal valine residue of the b-globin chain. Since the reaction rate is dependent on glucose concentration, a patient with uncontrolled diabetes mellitus (elevated blood glucose) has higher than normal concentrations of HbA1C.
The b-structure is highly resistant to protease digestion. Disulfide bonds serve to stabilize the native conformation in the extracellular space where physiologic conditions are more variable. Disulfide bonds are formed by the action of protein disulfide isomerase (located in the lumen of the endoplasmic reticulum) during folding of the polypeptide into its tertiary structure. Quaternary Structure Quaternary structure refers to the subunit composition of a protein (Fig. 3-5). Polypeptide subunits associate in a highly specific fashion to form a functional oligomer (oligo ¼ several; mer ¼ body).