生物化学资料：3-globular proteins.pptVIP

UNIT I Protein Structure and Function第一单元 蛋白质的结构和功能 Chapter 3 Globular Proteins 第3章 球状蛋白 II-E-3-c. Shift of the O2 dissociation curve II-E-3-d. Response of 2,3-BPG levels to chronic hypoxia or anaemia 2,3-BPG in the RBC increases in response to chronic hypoxia or anaemia. It helps to release of O2 from HbO2. II-E-3-e. Role of 2,3-BPG in transfused blood Storing blood in acid-citrate-dextrose leads to a decrease of 2,3-BPG The RBCs are able to restore their depleted supplies of 2,3-BPG only in 24-48hrs. The descrease in 2,3-BPG can be prevented by adding inosine being converted to 2,3-BPG. II-E-4. Binding of CO2 Some CO2 is carried as the following: Hb-NH2 + CO2 Hb-NH-COO- + H+ CO2-binding stablized the T or deoxy form of Hb. II-E-5. Binding of CO Tightly bind CO binds to one or more of 4heme sites, causing the remaining heme sites to bind O2 with high affinity. the curve left shift, hyperbola shape II-F. Minor hemoglobin II-F-1. Fetal Hb(Hb F) α2γ2(γbelongs toβ-F) Major Hb in the fetus newborn. Synthesis place: liver From the liver to the bone marrow, finally to RBC. Fetal Hb (α2γ2) has a higher affinity for O2 than maternal (adult) Hb . Hb F Hb A O2 placenta maternal fetal (positively charged AA ↓than Hb A) (2,3-BPG binding ↓) II-F-2. Hb A2 α2δ2(δbelongs toβ-F) Adult Hb, Minor(2-5%). Appearing about 12weeks after birth lower affinity for O2 than HbA II-F-3. HbA1C Nonenzymically glycosy-lated Hb A(α2β2-gluc.) Glucose groups attached to the NH2 of the N-end Val of βchains. Normal adult: HbA1C 3-9%; diabetes : HbA1C ↑ Higher affinity for O2 than HbA Two separate gene clusters, the α-gene family the β-gene family, are responsible for the code of different subunits of Hb There are temporal spacial specificity in their expression. Their organization shown in Fig III. ORGANIZATION OF THE GLOBIN GENES IV. HEMOGLOBINOPATHIES It is a kind of genetic defect that results in abnormal structure, insufficient quantities of the globin chain