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Proteins. By Emily Hodgson and Joshua Bower. Primary structure. The amino acid sequence. Secondary structure. Alpha helix Beta sheet. Tertiary structure. Folding of the protein. Quaternary structure. Multiple polypeptides e.g. collagen. Properties. Hypoalbuminaemia.
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Proteins • By Emily Hodgson and Joshua Bower
Primary structure • The amino acid sequence
Secondary structure • Alpha helix • Beta sheet
Tertiary structure • Folding of the protein
Quaternary structure • Multiple polypeptides • e.g. collagen
Properties Hypoalbuminaemia Liver disease (cirrhosis) Nephrotic syndrome Excess loss in bowel (protein-losing enteropathy, e.g., Ménétrier's disease) Burns (plasma loss in the absence of skin barrier) Redistribution (hemodilution [as in pregnancy], increased vascular permeability or decreased lymphatic clearance) Acute disease states Protein energy malabsorption Normal values = 3.5 - 5.0 g/dL 50% of protein content Negatively charged Produced in the liver only ALBUMIN Oncotic pressure Transport - hormones, bilirubin, free fatty acids, exogenous drugs, metals, ions pH buffer Negative acute phase protein Competitively binds Ca ions Dehydration High protein diet Functions Hyperalbuminaemia
Hypoalbuminaemia signs and symptoms • Leukonychia • Oedema and ascites (decreased oncotic pressure) • Jaundice • N.b. give lower doses of drugs as more will be free in plasm