1Polymers of amino acid
Proteins
2Proteins are synthesized in what part of the body?
Liver
3How many amino acids a typical protein have?
200-300 AA
4Smaller amino acids (<200)
Peptides
5Larger amino acids (>300)
Titin
6Proteins found in the muscles
Titin
7Macromolecules produced by the chains of amino acid
Proteins
8Dna-encoded genes are first used to produce mRNA
Transcription
9Synthesis of CHON from an mRNA template
Translation
10Processes involved in the protein synthesis
Transcription and Translation
11Where does transcription occurs in eukaryotic cells
Nucleus
12Is used as template to make mRNA
DNA
13Where does translation occurs
Ribosome in the cytoplasm
14In what process does the transfer of genetic instructions from DNA to mRNA occurs?
Transcription
15Contains genetic code which is read to make proteins
mRNA
16Central Dogma of Molecular biology
DNA - > RNA-> Protein
17Steps in Transcription process
Initiation, elongation, termination
18Beginning of the transcription process
Initiation
19What enzyme binds to the promoter during initiation?
Enzyme RNA polymerase
20What signals the DNA to unwind?
Binding of the enzyme and the promoter
21Complementary of the DNA
mRNA
22Addition of the nucleotides to make it longer
Elongation
23mRNA strand is complete and detaches from DNA
Termination
24Ending of transcription
Termination
25What are anabolic hormones
Thyroxine, Growth Hormone, Insulin & Testosterone
26Catabolic Hormones
Glucagon and Cortisol
27Hormones that participates in the synthesis of proteins
Anabolic
28Hormones involved to breakdown protein
Catabolic hormones
29Sum of all enzyme-catalyzed reactions in a living organism
Metabolism
31Destruction or breaking down
Catabolism
32Building block molecules are incorporated into larger, more complex molecules
Anabolic pathway
33Larger complex molecules into smaller molecules
Catabolic pathway
34Captured and used to drive anabolic rxns
Energy fraction
35Intake of nitrogen exceeds their loss as net protein synthesis proceeds
Positive nitrogen balance
36Pregnant women, growing children, and adults recovering from major illness
Positive nitrogen balance
37More nitrogen is excreted then incorporated into the body
Negative Nitrogen Balance
38Excessive tissue destruction, such as burns, wasting disease, continual high fevers, or starvation
Negative Nitrogen balance
39Less intake, greater elimination
Negative nitrogen balance
40Greater intake, less elimination
Positive nitrogen balance
41Difference between the intake and the output of nitrogen
Nitrogen balance
42Equal intake of nitrogen and the amount of nitrogen that was released outside the body
Nitrogen balance
43Reflect the equilibrium between the protein intake and the protein loss
Nitrogen balance
44Nitrogen excretion is greater than the nitrogen intake
Negative nitrogen balance
45Intake of nitrogen is greater than the output
Positive nitrogen balance
46Degradation of extracellular proteins or possible little intracellular degradation into the amino acid
Lysosomal pathway
47Degradation of intracellular proteins into an amino acid
Cytosolic pathway
48Two pathways that are necessary to convert intracellular proteins to free amino acids
Cytosolic and Lysosomal pathway
494 distinct levels of proteins structure
Primary, secondary, tertiary, quaternary
50Protein is losing its naturally occurring fold
Denaturation
51Factors that can denature proteins
Exposure to heat, hydrolysis with strong acid, hydrolysis with strong base, enzymatic rxn, exposure to urea and exposure to UV light
52Easiest structure to denature
Primary protein structure
53Structure that is most likely the hardest to denature
Quaternary protein structure
54What are the elements that consist proteins?
Carbon, oxygen, hydrogen, nitrogen, sulfur
55What sets protein apart from carbohydrates
Nitrogen
56Results from increased pH in the environment where the protein is exposed
Conversion of Carboxyl group to carboxylate and conversion of ammonium groups to amino groups
57pH at which an amino acid or protein has no net charge
Isoelectric point (pl)
58Number of positively charged groups equals the number of negatively charge group in protein
Isoelectric point
59What is the pH range of most proteins where isoelectric point occurs?
5.5 to 8
60What happens if the pH is greater than the isoelectric point?
Proteins will become negatively charged
61What happens if the pH is less than the isoelectric point?
Proteins will become positively charged
62Neutral pH
Proteins are negatively charged and that includes their charges at neutral pH
63Proteins that have charges on their surfaces
Hydrophilic
64What is the pH range required in solubility of proteins in blood
7.36-7.45 pH
65Where does solubility of proteins depend?
1. Number and the type of amino acid 2. Dependent on the pH of the environment, where these proteins are being exposed.
66What are the classification by protein function
Enzyme, hormones, transport proteins, immunoglobulins, structural proteins, storage proteins, energy source, osmotic force
67Catalyst of chemical rxn. Speeds up the chemical reaction
Enzymes
68Why do we have to avoid using hemolyzed samples
Bcoz constituents inside the rbc will be released in the plasma and will affect the results
69Proteins that act as chemical messenger
Hormones
70Controls the action of specific cell or a particular organ
Chemical messenger (Hormones)
71Hormone that promotes entry of glucose goint to the cell or it promotes the uptake of glucose going to the cell
Insulin
72Transport movement of ions, small molecules, or macromolecules
Transport protein
73Produced by the B cell of the bone marrow
Immunoglobulin
74Protects the body against foreign substances
Immunoglobulins
75Supports or help the structure and maintenance of the structure of the cells, in tissue like in tendons, and matrix of the bone.
Structural proteins
76Reserves of metal ions and amino acids
Storage proteins
78What will be the function of the storage proteins if they are needed Iike metal ions and AA
They will be mobilized and released in the circulation
79Reserve source of energy for tissue and muscles
Energy sources
80Alternative energy source
Proteins
81Conversion of proteins from the muscles and tissues into amino acids and then the amino acids will be converted to glucose
Gluconeogenesis
82Involved in the distribution of H2O throughout the body compartments
Osmotic force
83Does not allow proteins to cross the capillary membranes
Colloid osmotic force
84One of the signifcant function of proteins
Osmotic force
85Specific term for osmotic force
Oncotic pressure
86Do proteins have the ability to cross the capillary walls
No unlike other nutrients such as glucose, water, amino acids and oxygen. Proteins are only in the blood vessels
87Why can't proteins cross from the blood vessels to the capillary membrane to the tissues
Proteins macromolecules. They are large molecules and does have high oncotic pressure.
88What will happen if there is high oncotic pressure
There will be absorptiin of water from the tissues to the capillary walls or blood vessels
89Responsible in pulling water back from the tissues to the blood vessels
Oncotic pressure (possessed by our proteins)
90What will happen if there is low oncotic pressure
Abnormal accumulation of fluid in the tissues (edema)
91Retention of fluid in the tissues
Edema
92How does edema occurs
If there is an accumulation of fluid in the tissues because of decreased oncotic pressure
93What decreases oncotic pressure
If there is decreased plasma proteins.
94What causes decreased protein in the blood
Great loss of protein because of the damage in the kidney
95What generates large majority of oncotic pressure in capillaries
Presence of high quantities of albumin
96Considered to be the major plasma protein
Albumin
97What are the classification by protein structure
Database (manual), database (automated), simple proteins, conjugated proteins
98To provide a detailed and comprehensive description of the structural domains based on similarities of their amino acid sequences and three-dimensional structures
Database (manual)
99Utilizes four of the structural classifications
SCOP (Structural classification of proteins)
100What are the 4 of structural classifications
Class, fold, superfamily, family
101FSSP is also known as
Fold classification based on the structure-structure alignment of proteins
102Based on a three-dimensional structure comparison of protein structure in the Protein Data Bank
Database (Automated)
103Contains peptide chains composed of only amino acids
Simple proteins
104What are the shapes of simple proteins
Can be : Globular or Fibrous
105Globe like, round and symmetrical. They are easily dissolved in water (soluble in water)
Globular
106What proteins are classified under globular proteins
Enzymes, tranporters, hormones/messenger proteins
107Examples of globular proteins that are transport proteins
Albumin, Hemoglobin, Immunoglobulins
108Long, filamentous, asymmetrical (insoluble in water)
Fibrous proteins
109What makes fibrous proteins insoluble in water
R group of Fibrous proteins are hydrophobic (making them insoluble in water)
110Examples of proteins classified as fibrous proteins
Troponin, collagen
111Important for structural support of our connective tissues, tendons, bones, and muscles
Fibrous proteins (troponin, collagen)
112Can be detected or determined using electrophoresis
Major Plasma proteins
113Fraction of protein that migrates in a position faster than albumin towards the anode
Pre-Albumin
114Closest protein among all proteins in our body to the anode
Pre-albumin
115Has a significant role in the transport of vitamin A throughout the body
Pre-albumin
116Why is the function of Pre-albumin indirect in the transport of vitamin A
Bcoz Pre albunin does not directly bind with vit A
117Low level of Pre-albumin results to...?
Problems with the transport of vit A.
118Also involved in the transport of the hormone thyroxine
Prealbumin
119Another name of Pre-albumin
Thyroxine-binding Pre albumin (TBPA)
120What is the major transporter of thyroxine
Thyroxine-binding globulin
121What are the different conditions wherein prealbumin is decreased
Hepatic damage, acute-phase inflammatory response and Tissue necrosis
122Proteins present in highest concentration in the plasma
Albumin
123Responsible for nearly 80% of the colloid osmotic pressure of the intravascular fluid
Albumin
124Buffers pH and is a negative acute phase reactant protein
Albumin
125Major function of albumin
Colloid osmotic pressure
126Serves as a mobile repository of amino acids
Albumin
127Act as transport protein, a carrier protein
Albumin
128When can we use glycosylated albumin or the determination of fructosamine
Used to monitor glucose control for individuals with hemolytic anemia due to easy disintegration of their RBCs and the HbA1c cannot be longer used.
129Consists of a1, a2, B, and y fractions
Globulin
130Major component of a1 globulin
A1-Antitrypsin
131Enzyme involved in proteolysis
Protease
132Inhibitor of protease
A1-antitrypsin
133At what conditions A1-antitrypsin level is increased
Pregnancy, inflammatory conditions, use of contraceptives
134Largest major non-immunoglobulin protein found in the plasma and increased in nephrotic syndrome
A2 Macroglobulin
135What will happen to the a2 macroglobulins if there is nephrotic syndrome
Increased by 10 folds higher than the normal level
136Inactivates proteases
A2 macroglobulin
137Other major proteins that migrates in the a2 region
Haptoglobin
138Combines with Hgb to preserve body iron and protein store
Haptoglobin
139When is haptoglobin released
Released durinh lysis of cells, particulary RBCs in order to preserve iron store/level in the body
140What conditions increase haptoglobin
During stress, infection, acute inflammation, or tissue necrosis
141Life span of Haptoglobin
Half-life is about 4days if not bound to hgb
142Transferrin
Major beta globulin
143Transports ferric ions from the iron stores of intracellular or mucosal ferritin to the bone marrow
Transferrin
144Has an antibacterial effect by complexing iron
Transferrin
145Clot formation
Fibrinogen
146Lipid transport
B-lipoprotein
147Component of complement system
C3
148Surface immunity
Immunoglobulin A
149Binds to mast cells; hypersensitivity rxns
Immunoglobulin E
151Primary response; humoral immunity
IgM
152Single chain, globular, 153 AA
Myoglobin
153Primary O2 carrying protein
Myoglobin
154Used in conjuction with troponin to diagnose or rule out heart attack
Myoglobin
155Found in cardiac muscle
Myoglobin
156Has higher affinity to oxygen than oxygen to myoglobinqui
Hemoglobin
157Allowing early detection of acute myocardial infarction (AMI) / heart attack
Myoglobin
158Restoration of blood flow to a particular organ/tissue
Reperfusion
159Quickly open the block in the arteries by dissolving the clot or by quick restoration of blocked blood supply in the heart
Reperfusion
160What happens to the myoglobin once reperfusion is done
Myoglobin level decreases
161Something to do with the skelatal muscle
Rhabdomyolysis
162Due to vigorous exercise, elevatuon of myoglobin
Muscle trauma
163Progressive increase of myoglobin, can be toxic to the kidney
Renal failure
164Muscle weakness
Myopathies
165Elevated myoglobins due to vaccine
Intramuscular injection
166Tonic, stiffening of muscle; cloning, twitching/jerking of muscle
Seizures (tonic-clonic)
167Blockage in the blood flow
Arterial thrombosis
168Cardiac marker
Cardiac troponin (cTn)
169Specific to the heart muscles, in the striated muscle.
Cardiac troponin
170Gold standard in the diagnosis of acute coronary syndrome
Cardiac troponin
171Indicative of Myocardial injury
Increased troponin
172Troponin test is run for approx. ______
45 mins - 1hr
173What are cardiac markers
Myoglobin, Creatinine kinase (CK), CK-MB & troponin
174Replaces CK and CK-MB; more specific for detecting heart injury
Troponin I and Troponin T
175Not specific because they are present in the skeletal muscle along with myoglobin
CK and CK-MB
176Level of myoglobin 18 to 30 hrs after myocardial infarction or heart attack
Goes back to its normal level
177What happens to the troponin 18hrs to 30 hrs after myocardial infarction
Remain elevated for a longer period of time
178Increased CK, CK-MB and myoglobin, normal troponin
Either lesser degree of injury or the injury took place more than 24 hrs in the past
179Normal First troponin twst, all subsequent 6-12hrs troponin was tested again
Heart injury likely occurred w/in couple of hours prior to the first test and had not time to increase
180Normal CK-MB and Troponin, increased CK
Due to another cause such as skeletal muscle injury
181What is the advantage of troponin over the other cardiac markers
Troponin starts to decline to their baseline level about 5-10 days after the attack and is also dependent on how big the blood clot is
182Reference interval of cTnT
<0.1 ng/mL (mg/L)
183Value of equal to 0.1 could be consider____
There is damage already but in lesser degree
184cTnI cut off concentration for immunoassays
0.1 to 3.1 ng/mL (mg/L)
185It is produced in the kidney
Atrial natriuretic peptide
186Produced in the brain
B-Type (or brain) natriuretic peptide (BNP)
187Produced in the endothelium or endothelial cells
C-type natriuretic peptide
188Family of structurally related hormones that include Atrial natriuretic peptide, BNP, C-type and Dendroaspis natriuretic peptide
Natriuretic peptide
189Found in plasma and on cell surfaces
Fibronectin
190Synthesized in the liver hepatocytes, endothelial cells, peritoneal macrophages, and fibroblasts
Fibronectin
191Multifunctional glycoprotein; maintains adhesion
Fibronectin
192Important in tissue repair and regulating cell to cell attachment plus the motility of the cells
Fibronectin
193To predict the short term risk of premature delivery
Fetal fibronectin (fFN)
194Produced atthe boundary between the amniotic sac and the decidua
Fetal fibronectin
195Maintains the adherence of placenta to the uterus
Fetal fibronectin
196Glycoprotein that acts as a glue or adhesive between the lining of the uterus
Fetal fibronectin
197Cannot be detected after 24 weeks of gestation
Fetal fibronectin
198Good marker for impending labor (preterm labor)
Increased fFN r is detectable ate 24 weeks of pregnancy
199247 amin acid fat hormone produced by adipocyte
Adiponectin
200Composed of an N terminal collagen like domain and a C terminal globular domain
Adiponectin
201Individual is at greater risk to develop a heart disease, type 2 diabetes, metabolic syndrome and obesity
Decreased adiponectin
202Synonym prostaglandin D synthase; 168 amino acid
B-trace protein
203Accurate marker of CSF leakage
B-trace protein
204Not a diagnostic efficient test for glomerular filtration rate
B-trace protein
205Used as a sensitive marker in detecting renal function
B-trace protein
206Used to determine extent of damage in the kidneys
B-trace protein
207Better marker of kidney damageenal function
Cystatin
208Promising marker in the diagnosus of perilymphatic fluid fistulas
Cystatin
209What happens to the BTP in the blood if CSF leaks
Increased concentration of BTP
210Proteolytic fragments of collagen I formed during bone resorption (turnover)
Cross-linked C-Telopeptide (CTXs)
211Protein which is a producy of collagen breakdown
Cross-linked C-telopeptide (CTXs)
212The osteoclasts starts to breakdown the tissue in the bones to release the chemical present, particularly calcium which is to be transported into the blood
Bone resorption
213There is bone resorption ; greater breakdown of osteoclasts than normal
Increased CTXs
214How will we know that the therapy is effective?
If the conc. of the CTXs decreased by 35-55% from the baseline level
215Measurement of CTXs prior to therapy
Baseline level
216Prevents or slows down bone resorption
Antiresorption therapy
217Not a specific biochemical marker (cannot replace bone mineral density to diagnose osteoporosis)
CTXs
218Low molecular mass, 120 AA; cysteine proteinase inhibitor
Cystatin C
219More sensitive to diagnose or check any kidney damage
Cystatin C
220Completely fully reabsorbed and metabolized by the proximal tubule for recycling
Cystatin C