Coagulation system proteins → 12 coagulation factors (except Ca+)

Fibrinolytic system proteins: plasminogen, plasmin, activators, inhibitors

complement system

Immunoglobulin

lipoprotein

Plasma protein inhibitors

carrier protein

Plasma protein of unknown function

Albumin 50%, 38~48g/L

α1 globulin globulin 15~30g/L, clear/globulin=1.5~2.5

α2 globulin

beta globulin

gamma globulin

1. Most plasma proteins are synthesized in the liver, such as albumin, fibrinogen, fibronectin, exceptions: gamma globulin, plasma cells

2. The synthesis sites of plasma proteins are generally located on membrane-bound polyribosomes: liver, rough endoplasmic reticulum and Golgi complex, plasma membrane, and blood

3. Except for albumin, almost all plasma proteins are glycoproteins Blood group substances A and B are both composed of blood group substance O plus N-acetyl galactosamine or galactose.

4. Many proteins exhibit polymorphisms

5. Each plasma protein has its own specific half-life

6. Changes in plasma protein levels are often closely related to diseases.

1. Plasma functional enzymes

2. Exocrine enzymes

3. Cell enzymes

Such as the monocyte-phagocytic cell system, which engulfs plasma proteins and breaks them down into amino acids. Used in protein synthesis or converted into other nitrogen-containing compounds.

1. Rheumatism

2. Liver disease, prealbumin PAB is a sensitive marker of liver function damage Cirrhosis, decreased albumin, increased globulin, A/G inversion

3. Performance of total protein electrophoresis pattern of multiple myeloma (caused by malignant proliferation of plasma cells) ① A characteristic M protein peak appears in the original γ region, ② The albumin zone decreases

(1) Synthesis of δ-amino-γ-levulinic acid

(2) Synthesis of porphobilinogen

(3) Synthesis of uroporphyrinogen and fecal porphyrinogen

(4) Synthesis of heme

Heme is an allosteric inhibitor of ALA synthase Pesticides can induce the production of ALA synthase Heme can inhibit the expression of ALA synthase VB6 lacks the activity to inhibit ALA enzyme

Heavy metals (lead) inhibit ALA dehydratase and ferrochelatase Inhibition of heme synthesis is an important sign of lead poisoning.

EPO can be combined with primitive red blood cells (such as erythroid burst colony-forming unit BFU-E) and Erythroid colony-forming units (CFU-E) interact to accelerate nucleated red blood cell maturation and the synthesis of heme and Hb.

Abnormal synthesis and metabolism of iron porphyrins leads to increased excretion of porphyrins or their intermediate metabolites, which is called porphyria. It is divided into congenital and acquired. Congenital is caused by a genetic defect in a certain heme synthase system. Acquired, mainly refers to lead poisoning Or iron porphyrin synthesis disorders caused by certain drug poisoning, such as lead and other heavy metal poisoning. Also inhibits uroporphyrin synthase.

(1) Glycolysis is the only way for red blood cells to obtain energy Physiological activities maintained by ATP

2. There is a 2,3-bisphosphoglycerate bypass 2,3-BPG branch in the glycolysis of red blood cells, which only regulates the oxygen transport function of hemoglobin.

(3) The pentose phosphate pathway provides NADPH (only) to maintain the integrity of red blood cells and maintain the content of reducing glutathione GSH.

(4) Red blood cells cannot synthesize fatty acids

(5) Heme promotes the synthesis of globin

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