Objectives for today: describe how erythrocytes (red blood cells) and neutrophils are derived from stem

m cells in bone marrow. describe and explain how erythrocytes and neutrophils are specialised for their functions.

Syllabus: 1.1.3 some more of h & i

describe the role of haemoglobin in carrying oxygen and carbon dioxide.

Syllabus: 1.2.2 l
http://www.youtube.com/watch?v=gP93ztoXuYw http://www.youtube.com/watch?v=MgVPLNu_S-w&feature=related

Homework: finish questions not completed in class. Now:

Blood Water
Plasma Plasma proteins (for blood clotting and maintaining low water potential of blood) 50-60% Ions, e.g. Na+ Ca2+ Cl- Digested food, e.g. amino acids, fatty acids, glucose Metabolic wastes e.g. CO2 & urea. Hormones, e.g. testosterone, ADH, insulin

Red blood cells (erythrocytes) 38-48% Cells White blood cells (leucocyte) 2-3% 40-50% Platelet (thrombocyte ) 1%

Neutrophils A multi-lobed nucleus: 3-4 lobes. Many vesicles containing hydrolytic enzymes and hydrogen peroxide.

Erythrocytes Biconcave shape & small size means high surface area to volume to ratio for rapid diffusion of oxygen and CO2 Haemaglobin forms reversible reaction with oxygen: oxygen + haemaglobin oxyhaemaglobin Haemaglobin forms reversible reaction with 10-20% of the CO2 in your blood: CO2 + haemaglobin carbaminohaemaglobin No nucleus, mitochondria or ER so more space for haemaglobin.

And now: Fill in the gaps in the How are neutrophils and erythrocytes derived from stem cells? sheet.

Extension: Try SAQ 11 & 12 on p.80 of the green books. Answers on p. 248.

multipotent differentiate changes specific function phagocytosis lysosomes enzymes size shape organelles gene expression mitosis

Haemoglobin Hb loads and unloads one oxygen molecule at a time so can exist as: Hb, HbO2, HbO4, HbO6, or HbO8. The term % saturation means the overall loading of Hb molecules with oxygen: how much of the maximum possible oxygen is being carried by Hb?

Cooperative binding The binding of oxygen molecules to haemaglobin alters the shape of the protein slightly (a conformational change). This change in shape makes it easier for haemaglobin to bind additional molecules of oxygen, i.e. the 2nd, 3rd and 4th oxygen molecules each bind more easily than the last one did. When one oxygen molecule has been released, the shape of haemaglobin changes back slightly so releasing the 2nd, 3rd and 4th oxygen molecules more easily.

Oxygen dissociation curve 100

% saturation of haemalobin

Plateau: Haemaglobin has a high affinity for O2 so becomes highly saturated and therefore loads up with O2 in the lungs.
Steep slope: A small drop in O2 concentration causes haemaglobin to have a much lower affinity for O2 The haemaglobin is less saturated with O2 so releases it more easily at the tissues.

Body tissue

lungs

partial pressure of O2 (mmHg)

And now: 1. Read the haemoglobin disassociation curve bit on p.80-81 in the green books & p.64-65 in the purple books. 2. Do the questions on your handout anything you dont finish in class is homework!