Topic 4: Functions, fractination and changes of Plasma Proteins Flashcards

1
Q

What should be mentioned in this topic?

A
  • Synthesis
  • Functions
  • Fractionation
  • Pathological Changes
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2
Q

Synthesis:

A

Almost all the proteins are synthesised in the liver except for gamma globulins, HDL and VLDL and i.c. enzymes

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3
Q

Functions:

A
  • Maintaining oncotic pressure (albumin, keeps water in circulation)
  • Transport functions of Albumin
  • Transport functions of globulins
  • Lipids bind to proteins forming lipoproteins
  • Blood sedimentation
  • Buffer
  • Blood clotting
  • Immunity
  • Enzymes in the plasma (hormone inactivation, diagnostic importance)
  • Protein metabolism (change constantly)
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4
Q

Functions:

Transport functions of Albumin:

A
  • Fatty acids
  • Bilirubin
  • Hormones
  • Vitamins
  • Metal ions
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5
Q

Functions:

Transport functions of globulins:

A
  • Transferrin
  • Haptoglobin
  • Transcortin
  • Thyroxin Binding Globulin - Transcobalamin
  • Lipoproteins
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6
Q

Functions:

Lipids bind to proteins forming lipoproteins:

A
  • VLDL
  • LDL
  • IDL
  • HDL
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7
Q

Functions:

Blood sedimentation

A
  • Clinical parameter
  • In case of infections acute phase proteins appear in the plasma.
  • These are produced by the liver
  • Bind to the surface of red bloods cells reducing the charge, causing less repulsion
    between the red blood cells and thus sedimentation becomes faster.
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8
Q

Functions:

Buffer action:

A

Plasma proteins are responsible for 7% buffer capacity of blood, 15% buffer capacity of the plasma

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9
Q

Functions:

Blood clotting

A
  • All of the factors involved in blood coagulation except for Ca2+ circulate in the
    intravasal compartment as inactive precursors
  • Also responsible for anticoagulation and fibrinolysis
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10
Q

Functions:
Immunity:

A
  • Immunoglobulins
  • Proteins of non-specific immunity
  • Signal proteins and peptides
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11
Q

Fractionation:

A
  • Paper electrophoresis
  • Gel electrophoresis
  • Immunoelectrophoresis
  • Ion Exchange chromatography
  • HPLC
  • Ultracentrifugation
  • Gel-filtration
  • Affinity Chromatography
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12
Q

Fractionation:

Paper electrophoresis

A

Only Albumin and Fibrinogen can be separated with this method. The rest of the
proteins can be found in the globulin fraction.

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13
Q

Fractionation:

Gel electrophoresis

A

Seperated into albumin, and globulins (a1, a2, b, g)

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14
Q

Fractionation:

Immunoelectrophoresis

A

Antibody distributed in a gel poured on a sheet of glass develops precipitation arcs with the antigen in the electric field

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15
Q

Fractionation:

Ion Exchange chromatography

A

Separates proteins on the basis of their charge

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16
Q

Fractionation:

HPLC

A

High Pressure Liquid Chromatography: divides proteins in a solid phase column
under high pressure perfusion

17
Q

Fractionation:

Ultracentrifugation

A

Spinning tubes at high G to separate macromolecules according to their sedimentation constants

18
Q

Fractionation:

Gel-filtration

A

Smaller molecules have to pass through the polysaccharide beads and hence move
slower than bigger beads which just bypass the beads.

19
Q

Fractionation:

Affinity Chromatography

A

One covalently binds a specific antibody formerly produced against the protein to the granules of the solid phase. The proteins will then be selected from the mixture by a special recognizing system.

20
Q

Pathological Changes

A
  • Hypo and Hyperproteinemia
  • Dysproteinemia
  • Paraproteinemia
  • Defect-proteinemia
21
Q

Pathological Changes:

Hypo and Hyperproteinemia

A

Brought about by starving, kidney disease

22
Q

Pathological Changes:

Dysproteinemia

A

Ratio changes

23
Q

Pathological Changes:

Paraproteinemia

A

Pathological proteins appear

24
Q

Pathological Changes:

Defect-proteinemia

A

Lack of some of the fractions