Hemoglobin , myoglobin Flashcards by Amelia C

what is metalloprotein

structural component is a metal element

they are also examples of heteroproteins
they can also be called hemoproteins

structure is protein ( globin ) + heme ( prosthetic group )

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metal ion binds directly to which polypeptide chains

Fe3+ - transferrin, ferritin
Cu2+ - cerruloplasmin, cytochrome oxidase
Zn2+ - lactate dehydrogenase, alcohol dehydrogenase, carbonic anhydrase
Ca2+ - calmodulin
Mg2+
, Mn2+…

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Give some examples of prosthetic groups with metal ions in them

Fe2+ - myoglobin, haemoglobin
Fe3+ - cytochromes, catalase, peroxidase

it makes up the prosthetic group heme

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iron ( fe 2plus ) what can you tell me about it

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what is myoglobins function

Function: oxygen carrier and reservoir - in tissues which require large oxygen
reserves for periods when energy demands are high – skeletal muscle, heart

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what is the structure of myoglobin

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what is the function of haemoglobin

Function: oxygen transport from lungs via blood to tissues → transport via erythrocytes
- reason: solubility of O2 in blood/plasma very low, diffusion very slow
→ Ery – 300.106 Hb

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what is the structure of haemoglobin

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how is the quaternary structure of haemoglobin formed

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what is myoglobins most important function

in the muscle

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what is the haemoglobins most important function

in the lungs

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describe the hyperbolic binding curve of MB

hyperbolic binding curve = high affinity to O2
 inefficient unloading in tissues
leads to
efficient O2
storage

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describe the hyperbolic binding curve of HB

Hb
- sigmoidal binding curve
 efficient O2 binding (high affinity)
in lungs, efficient unloading
(low affinity) in tissues
leads to
efficient O2
transport

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what is the sigmodial binding curve of Hb

2 kinds of structures basing on conditions

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what causes the transition of tense to relax conformation in HB

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what is the mechanism of the t to r transition in hb
roughly

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what is the mechanism of the t to r transition in hb
roughly ( steps )

The binding of O2 to deoxyHb causes conformational change in the heme:

in the deoxy state heme molecule has a dome shape
binding of the O2 to Fe2+ pulls the iron into the heme plane
flattening the heme and causing strain
a shift in the orientation of His F8 relieves the strain, because Val FG5 is
pushed to the right

 the change in heme is communicated to the FG corner of a subunit 
induces conformational shifts at  -interface  oxy conformation =
strong-binding (R)stat

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what can change HB’s ability to bind and release oxygen

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how do protons affect Hb-o2 affinity

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how does carbon dioxide affect the o2 affinity

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how does BPG affect O2 affinity

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how does bgp bind to deoxy hb

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how does oxygen transport from mother to fetus

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how much do the allosteric factors - h. co, bpg affect oxygen affinity

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what are the minor forms of Hb - Haemoglobin A 1 c

what variants of hB how can we identify them

what is sickle cell anemia , what happens exactly

what are immunoglobins and what is there function

Important elements of humoral immune response * Globular glycoproteins, well soluble in water * ~ 20-30 % of total plasma proteins, present also in other body fluids * Produced by B lymphocytes (B cells) in response to presence of antigens * Function: bind antigens and target them for destruction

what is an antigen , what is antigen determinants

* Antigen = „antibody generator“ = any molecule or particle identified as foreign capable of inducing a specific immune response - viruses, bacteria, fungy, tissue cells, large molecules – proteins, polysaccharides, glycoproteins, lipoproteins, nucleic acids, … * Antigenic determinants (epitopes) - the specific small piece of the antigen to which an antibody binds ~ specific sequences of amino acids or a carbohydrate residue (oligosaccharide) - each antigen molecule contains several epitopes

what is hapten

Hapten – small molecule attached to a large carrier protein – may act as antigen and elicit an immune response (a carrier-free hapten is not immunogenic)

what is the immunoglobulin structure

antigen and antibody complex

what are the immunoglobulin classes and functions how many types of heavy chains and light chains whats the Ig function

what is the mechanism of action IgG

what is the mexchanism of action IgE

how can we use immunoglobulins in medicine

* Diagnostic markers * Analytical reagents in immunoanalysis - Antibody-antigen interaction = the basis for a variety techniques that specifically identify and quantify specific components in a complex sample *Therapeutical agents – cancer, inflammatory diseases, autoimmune diseases

types of antibodies ( just the names )

polyclonal monoclonal

polyclonal antibodies in more depth