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protoporphyrin-IX + Fe2+ (planar) O2 and His residue stick up/down from planar molecule |
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form of iron when carrying oxygen? |
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Fe2+, will not release oxygen to tissues in 3+ form |
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oxygen carrying molecule in cells 1 heme plus 8 alpha helices connected by bends |
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similar to Mb but have hydrophobic patches that associates w/ other subunits in heterotetramer |
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concentration at which 1/2 ligand sites are bound -> higher Kd = tighter binding |
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metabolic effectss on O2 delivery |
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O2 binds less tightly at lower pH due to protonation and subsequent conformational change of His residue... metabolism produces lactic acid and increases O2 delivery |
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hemoglobin molecule + 4 CO2 molecules in readily reversible noncovalent adduct to transport back to lungs; forms/ disassembles based on CO2 concentrations |
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maintains T state by adding more ionic bonds, which lowers affinity for oxygen; higher levels in tissues at higher altitudes to achieve higher dump rate and maintain overall oxygen delivery |
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lower affinity for BPG and higher affinity for O2 than adult Hb; alpha 2 gamma 2 structure |
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embryonic hemoglobin produced early in embryonic development; epsilon 2 zeta2 structure |
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functions in erythropoeisis to call signaling that differentiates marrow cells into erythrocytes; EPO binds to this complex to initiate signaling pathway |
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prostaglandin vasoconstrictor that activates GPIIa/GPIIb after synthesis by activated platelet; synthesis inhibited by low-dose aspirin |
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down-regulating "buddy" is Thrombomodulin; once activated also activates V to Va and VIII to VIIIa, accelerating its own activity |
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1. multiple intrinsic factors or factor VIIa/TF complex from extrinsic pathway activate IX to IXa 2. IXa + VIIIa activate X to Xa |
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1. trauma causes TF to activate VII to VIIa 2. VIIa + TF activate X to Xa |
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1. Xa + Va converts prothrombin to thrombin (Factor II to IIa) 2. Thrombin converts Fibrinogen to Fibrin (Factor I to Ia) |
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prothrombinase complex components |
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Definition
Va + Xa + II (prothrombin) |
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converted by thrombin to XIIIa; transglutaminase that covalently links Gln to Lys in aggregates of fibrin clot to form hard clot from soft clot |
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calcium in clotting pathway |
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Definition
calcium covers phospholipids exposed by tissue damage; some coag factors post-translationally modified w/ gamma-carboxyl grps to bind w/ Ca -- leads to localization; gamma-carboxylation requires Vit K as a cofactor; Warfarin (Vit K analog) inhibits this process |
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non-covalent inhibition of clot formation |
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Definition
tissue factor pathway inhibitor (TFPI) antithrombin III (ATIII) proteins Z and ZPI |
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covalent inactivation of protein cofactors |
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activated protein C (w/ protein S and thrombomodulin |
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binds Xa and "turns off" extrinsic pathway complex |
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type of serpin (serine protease inhibitor) binds irreversibly/inhibits Factors Xa, IIa, IXa, XIa; heparin stimulates this inactivation |
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1. captures escaped thrombin 2. in absence of fibrinogen TM-thrombin complex converts Protein C to Ca 3. Protein Ca complexes w/ Protein S to inactivate Factor Va and Factor VIIIa 4. clotting is regulated |
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tissue plasminogen activator-hydrolyzes plasminogen to plasmin |
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protein inhibitor of plasmin |
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aka urokinase; exogenous protein that happens to hydrolyze plasminogen to plasmin |
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active protease that hydrolyzes fibrin |
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foreign molecules bound selectively by antibodies |
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molecules that produce antibody production |
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small region of a larger molecule that elicits production of specific antibody; aka epitope; may be only 6-7 AAs in proteins |
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5 classes of immunoglobulins |
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IgG- most abundant, fights microbes IgA- mucosal secretions, external protection; may form dimer IgM- forms pentamer; early in infection IgD- leukocytes IgE- immunity to parasites; allergies correspond to 5 different heavy chain types; coupled w/ EITHER kappa or lambda |
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two layers of beta-sheets with hydrophobic residues "sandwiched" together; type of super secondary structure; 7 and 9 sheet versions (antigen binding domain is 9 sheet version) |
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HVR is area of variability between aka complementarity determining region (CDR); relatively constant AA structures; form antigen binding site at top and center (cleft) |
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enzyme-linked immunosorbent assay; uses antibodies against antigen of interest to perform assay |
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