Hemoglobin and iron metabolism. Flashcards

1
Q

hemoglobin LIST

A

structures
functions
types
clincials
measurements

she
found
two
cute
monsters

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2
Q

hemoglobin - structure 1

A

hemoglobin is a tetramer protein meaning made of 4 polypeptide chains

HemoglobinA = x2 alpha subunits
HemoglobinB = x2 beta subunits

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3
Q

hemoglobin - structure 2

A

1 hemoglobin = 4 subunits = 4 heme group = iron centre = x1 oxygen binded

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4
Q

hemoglobin - function 1

A

OXYGEN TRANSPORT

hemoglobin + oxygen = oxyhemoglobin (lungs)

reaching tissues/ organs

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5
Q

hemoglobin - function 2

A

CARBON DIOXIDE TRANSPORT

hemoglobin + carbon dioxide = carbo-amino-hemoglobin

  • reaches lungs
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6
Q

hemoglobin - function 3

A

BUFFERING

hemoglobin acts a as buffer to maintain correct blood pH levels in terms of H+/HCO3=

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7
Q

hemoglobin - function 4

bohr effect 1

A

BOHR EFFECT

  • more co2 -> diffuses into blood
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8
Q

hemoglobin - function 4

bohr effect 2

A
  • co2 + h2o = h2co3 = lowers blood pH
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9
Q

hemoglobin - function 4

bohr effect 3

A
  • hemoglobin has less affinity to bind to oxygen, so oxygen is left behind + released into tissues
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10
Q

hemoglobin - function 4

bohr effect 4

A
  • oxygen dissociation curve turns right
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11
Q

hemoglobin - function 4

bohr effect 5

A

ensures active tissues producing more co2 get more o2-> to improve efficiency of o2 transport

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12
Q

hemoglobin - function 5

A

HALDANE EFFECT

when hemoglobin binds to oxygen = changes shape

Hb now so less affinity for co2

Hb better at picking up co2 to be taken back to lungs

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13
Q

hemoglobin - type 1

A

ADULT HEMOGLOBIN

  • HemoglobinA = x2 chains
  • HemoglobinB = x2 chains
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14
Q

hemoglobin - type 2

A

FETAL HEMOGLOBIN

  • HemoglobinA = x2 chains
  • HemoglobinF = x2 chains

HbF has higher affinity for oxygen than HbA = oxygen transfer from mother -> foetus

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15
Q

hemoglobin - type 3

A

SICKLE HEMOGLOBIN

HemoglobinS
- abnormal variant for sickle cell anemia
- caused by point mutation of HBB gene on chromosome 11
- valine overtakes glutamic acid on position 6 of HemaglobinB chain

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16
Q

hemoglobin - clinical 1

A

ANEMIA

  • due to insufficient Hb levels to transport iron around body
17
Q

hemoglobin - clinical 2

A

CO POISONING

  • hemoglobin binds to CO = carboxyhemoglobin
    = no O2 transport as CO taken all Hb bindings
18
Q

hemoglobin - measuring

A

normal Hb levels = 15g/dL

hemoglobin electrophoresis

19
Q

iron metabolism - LIST

A

sources
absorption
transport
usage
recycling

clinicals

20
Q

iron metabolism - 1

A

SOURCES

heme iron
- animal meat products
- small intestine epithelial cells (enterocytes) of upper duodenum

non heme
- plant grain products
- Fe3+ -> Fe2+ reduced duodenal cytochrome B and uptaken by DMT1

21
Q

iron metabolism - 2

A

ABSORPTION

hepcidin = liver based hormone controlling iron absorption/ release

too much iron = more hepcidin = less absorption

22
Q

iron metabolism - 3

A

TRANSPORT

iron id transported by proteins

trans-ferrin binds to Fe3+ to take to tissues/ organs

lacto-ferrin found in mucosal secretions for immune function

23
Q

iron metabolism - function 4

A

STORAGE

ferritin = excess iron storage = ferritin
hemos-iderin = complex of excessive iron storage

24
Q

iron metabolism - 5

A

USAGE

  • hemoglobin synthesis in reduced form
25
Q

iron metabolism - 6

A

RECYCLING

iron is recycled by macrophages in spleen/ liver

26
Q

iron metabolism - clinical 1

A

IRON DEFICIENCY

  • pregnancy
  • growth
  • bad diet

= anemia

27
Q

iron metabolism - clinical 2

A

IRON OVERLOAD

iron supplements = liver damage