Plasma proteins, the components of plasma proteins, the protein fractions and condition causing the alteration in the each protein fraction. Clinical implications of the each fraction, the electrophorotic pattern of plasma protein. Acute phase proteins which include the positive and negative phase proteins.
Plasma Proteins For Therapeutic Use; An Introduction to Blood PLASMA & its Se...Maryam Pazireh
An INTRODUCTION TO PLASMA & its Separation Methods;
what is Plasma & its composition, What does it do in the body, and Plasma Proteins as pharmaceutical crops
This powerpoint contains details regarding detoxication reactions of xenobiotics. Examples of reactions of different phases of detoxication has been given.
A brief discussion on cytochrome P450 is also included.
Enzymes and Nucleic acids recap-AS Biology [JM]Jorge Pinto
Aim: explore and the structure and function of enzymes
Objectives:
List the main properties of enzymes
Explain the terms active site, specificity and catalysts
Discuss how enzyme activity is affected by temperature and pH
Plasma proteins, the components of plasma proteins, the protein fractions and condition causing the alteration in the each protein fraction. Clinical implications of the each fraction, the electrophorotic pattern of plasma protein. Acute phase proteins which include the positive and negative phase proteins.
Plasma Proteins For Therapeutic Use; An Introduction to Blood PLASMA & its Se...Maryam Pazireh
An INTRODUCTION TO PLASMA & its Separation Methods;
what is Plasma & its composition, What does it do in the body, and Plasma Proteins as pharmaceutical crops
This powerpoint contains details regarding detoxication reactions of xenobiotics. Examples of reactions of different phases of detoxication has been given.
A brief discussion on cytochrome P450 is also included.
Enzymes and Nucleic acids recap-AS Biology [JM]Jorge Pinto
Aim: explore and the structure and function of enzymes
Objectives:
List the main properties of enzymes
Explain the terms active site, specificity and catalysts
Discuss how enzyme activity is affected by temperature and pH
Adverse drug reactions (ADRs) are untoward effects of drugs that are given in conventional therapeutic settings. These reactions are extremely common in the practice of medicine and are believed to affect 7% to 8% of patients admitted to a hospital. About 10% of such reactions prove fatal .
Diuretics and antidiuretics detail STUDYNittalVekaria
diuretics and antidiuretics detail study
-diuretic are the drug which increase the urine formation and excretion.
- antidiuretic work by decrease the urine formation.
classification, mechanism of action, use ,pharmacokinetic, pharmacodynamic,adverse effect
-newer drug
-banned diuretic and antidiuretic drug
Diuretics, sometimes called water pills, help rid your body of salt (sodium) and water. Most of these medicines help your kidneys release more sodium into your urine. The sodium helps remove water from your blood, decreasing the amount of fluid flowing through your veins and arteries.
Types of diuretics include:
Thiazide diuretics, such as hydrochlorothiazide (Microzide® or Oretic®) or chlorthalidone (Hygroton® or Thalitone®).
What they do: They make your kidneys pull salt and extra water into your pee.
Selected side effects:
Headache.
Loss of appetite.
Hair loss.
Loop diuretics, such as furosemide or bumetanide
What they do: They affect part of your kidneys (the loop of Henle) to get salt and excess water out of your body.
Selected side effects:
Dizziness.
Diarrhea.
Upset stomach.
Potassium-sparing diuretics, such as triamterene or amiloride
What they do: They help your kidneys clear salt and water out of your body, but don’t let you lose too much potassium in the process.
Selected side effects:
Gas.
Nausea.
Headache.
A mixture of two types in one pill, like triamterene and hydrochlorothiazide (Dyazide® or Maxzide®)
What they do: They make your kidneys move salt and extra water out while keeping you from losing too much potassium.
Selected side effects:
Headache.
Peeing often.
People usually take diuretics by swallowing diuretic pills, but your provider can give some diuretics through an IV in your arm during a hospital stay. Most people can take diuretics without getting serious problems from them.
How do diuretics work?
Diuretics make your kidneys take away your body’s extra salt and water by putting them into your urine (pee).'
1 Medical uses
2 Types
2.1 High-ceiling/loop diuretics
2.2 Thiazides
2.3 Carbonic anhydrase inhibitors
2.4 Potassium-sparing diuretics
2.5 Calcium-sparing diuretics
2.6 Osmotic diuretics
2.7 Low-ceiling diuretics
3 Mechanism of action
4 Adverse effects
5 Abuse in sports
6 See also
7 References
4. • Coenzymes transferring groups other than H
– Biotin (CO2)
– Pyridoxal phosphate (amino)
– CoA (acyl)
– Tetrahydro folic acid (1 C groups)
– Methyl cobalamine (CH3)
– ATP (PO4)
– S Adenosyl methionine (CH3)
– UDP (glucose/galactose)
• Last three do not belong to Vitamin B complex
5. • Activators are metal ions
– tightly bound- metalloenzymes
– loosely bound- metal activated enzymes
• Stabilise proper conformation
• Cu2+ for tyrosinase, Mg2+ for kinases
• Fe, Cu in oxidation-reduction reactions
• Pyruvate dehydrogenase complex requires 5
activators: Mg2+, NAD+, FAD+, TPP, CoA
• Xanthine oxidase requires FAD, Mo, Fe
6. • Multifunctional enzymes: same enzyme
molecule having different functions for
different parts of that enzyme molecule
– fatty acid synthase complex
• Multienzyme complex: many enzymes
clustered together having common function
7. • Active site of lysozyme:
Glu Asp Trp Trp Asp
35 52 62 63 101
Catalytic site substrate binding site
• Hexokinase- 0.02 mmol L-1 : always active
• Glucokinase- 10 mmol L-1 : only when glucose
concentration is high, only in liver
8. CLINICAL APPLICATIONS OF COMPETITIVE INHIBITION
• Sulphonamides(NH2-C6H5-SO2-NH2) resemble
PABA (NH2-C6H5-COOH), hence inhibits it
• Anticancer drugs like methotrexate,
aminopterin inhibit dihydrofolate reductase
• Alcohol dehydrogenase catalyses conversion
of methyl alcohol to formaldehyde. Ethyl
alcohol inhibits it. Therefore ethyl alcohol is
used during methyl alcohol poisoning.
9. • Allopurinol is used to treat gout as it inhibits
xanthine oxidase that converts hypoxanthine
to uric acid
• Dicoumarol is an anticoagulantas it inhibits
Vit K needed for coagulation
• Lovastatin inhibits HMG-CoA reductase, hence
used to reduce cholesterol level in blood
10. NONCOMPETITIVE INHIBITORS
• Cyanide inhibits cytochrome oxidase
• Iodoacetate inhibits enzynes having –SH
(sulfhydryl) group at active site like
glyceraldehyde-3-phosphate dehydrogenase
• Fluoride inhibits enolase (binding with Mg 2+
or Mn2+)
• Di-isopropyl fluorophosphate (DFP) inhibits
enzymes having serine at active site like
chymotrypsin, acetylcholine esterase
11. SUICIDE INHIBITION
• Irreversible
• Mechanism based inhibition
• Allopurinol becomes alloxanthine which is a
more potent inhibitor
• 5-fluoro uracil becomes fluoro deoxy uridylate
which binds to the enzyme thymidylate
synthetase and inhibits it
12. ALLOSTERIC MODULATION
• Regulation of enzyme activity in the body
• Positive & negative modulators
• Not a substrate analog
• Reversible
• Allosteric site other than active site
• Brings about conformational change
• Mostly oligomeric enzymes
– Aspartate transcarbamoylase (6 polypeptide chains)
– Pyruvate kinase (4 polypeptide chains)
13. • Have sigmoidal curve
ENZYME INHIBITOR ACTIVATOR
ALA synthase heme
phosphofructokinase ATP, citrate AMP
Aspartate transcarbamoylase CTP ATP
14. UNCOMPETITIVE INHIBITION
• Cannot bind with free enzyme, only to E-S
complex
inhibitor
• 1/V
1/S
• Eg,. Inhibition of placental alkaline
phosphatase (Regan isoenzyme) by phenyl
alanine
15. REGULATION OF ENZYME ACTIVITY
• Induction (depression) and repression
– Some are constitutive enzymes like hexokinase
– Others are inducible like glucokinase
• Allosteric modulation
• Covalent modulation
– Zymogen activation, phosphorylation and
dephosphorylation
• Compartmentalisation of pathways
• Degradation
• isoenzymes
16. DIAGNOSTIC ENZYMES
• Aspartate transaminase
– Normal 2 – 40 IU/L
– Increases during MI & liver diseases
• Alanine transaminase
– Normal 0 – 45 IU/L
– Very high during liver diseases
– Moderately high during MI
17. • Alkaline phosphatase
– Hydrolysis of phosphate esters
– Optimum pH 9.5-10
– 25-100 IU/L
– Increases in liver & bone diseases
– Very high in cholestatic/obstructive jaundice
• Acid phosphatase (prostatic fraction)
– Optimum pH 4.5
– Increases in bone diseases & prostate cancers
– Prostatic specific antigen-protease
• 5mg/L
• 4 to 10mg/L benign; >10 mg/L cancerous
18. • 5’ nucleotidase
– Normal 2-10 IU/L
– High in liver diseases, very high in cholestasis
• γ- glutamyl transpeptidase
– Normal 10-30 IU/L
– High in liver diseases, very high in alcoholics
• Cholinesterase
– Normal 2-121 IU/L
– Inhibited by organophosphorous pesticides
• Pseudocholinesterase
– Decreases in liver diseases
19. • Amylase
– Normal 50-120 IU/L
– Very high in acute pancreatitis
– Moderately high in chronic pancreatitis & mumps
• Lipase
– Normal 0.2-1.5 IU/L
– Diagnostics same as above; also high in cholestasis
20. THERAPEUTIC ENZYMES
• Streptokinase
– To dissolve intravascular clots
• Asparginase
– To treat leukemia
• Pancreatin
– Lipase, trypsin
– To treat pancreatic insufficiency
• Collagenase
– To remove scar tissue