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34 Cards in this Set

  • Front
  • Back
What is heterochromatin?
DNA that's condensed tightly.
Transcriptionally inactive.
What is euchromatin?
loosely condensed DNA
genes can be transcribed
In what direction is DNA/RNA synthesized?
The 5' end of the incoming nucleotide (has the triphosphate used to make the bond) binds to the 3' end of the elongating chain.
How is mRNA read?
It is READ in the 5' to 3' direction.
In protein synthesis, which end of the incoming amino acid adds to which end of the growing chain?
The N-part of the incoming AA adds to the C-part of the elongating chain.
What is the mRNA start codon?
AUG
What are the stop codons for mRNA
UGA, UAA, UAG
What does RNA pol-I do?
Makes ribosomal RNA (rRNA) for eukaryotes
What does RNA pol-II do?
Makes mRNA for eukaryotes
What does RNA pol-III do?
Makes tRNA for eukaryotes
How does the Golgi 'tag' proteins for distribution to the lysosome?
It adds mannose-6-phosphate, which 'packages' protein for delivery to lysosome.
What is clathrin?
Protein that directs vesicles to be sent to specific places.
If from Golgi → lysosome.
If from plasma membrane → endosomes (means of receptor mediated endocytosis).
Discuss structure of microtubules
Made of 9 + 2 polymerized alpha & beta tubulin dimers.
Dynein & Kinesin
Dynein: transports stuff retrograde on microtubule.

Kinesin: transports stuff forward on microtubule
What is the defect assoc. with Chediak-Higashi syndrome?
microtubule polymerization defect
Type-I collagen
found in bone, skin, and tissue
type-II collagen
found in cartilage
type-III cartilage uses
skin, blood vessels, uterous, granulation tissue

defective in Ehlers-Danlos
type-IV cartilage use
*IMPORTANT
found in basement membrane of tissue

Defective in Alport's syndrome
How is collagen processed?
In the fibroblast, it is synthesized in the RER, then hydroxylated (req. vitamin C) & glycosylated in the ER, before it's exocytosed as procollagen

Outside the fibroblast, it's proteolytically cleaved into tropocollagen before X-linked into collagen fibrils
Elasting: discuss it
stretchy; found in lungs, large arteries, leastic ligaments, etc

lots of Pro and Gly

broken down by elastase, which is inhibited by alpha1-antitrypsin

Defective in Marfan's syndrome
What is Southern blot?
DNA tagged with labeled DNA
what is Northern blot
RNA tagged with labeled DNA
Western Blot
Protein separated by gel electrophoresis and tagged with radioactive Ab
How does ELISA work?
Patients serum is mixed with labeled agent (to determine if pt has Ab against it) or with labeled Ab (to see if antigen is present)
What is imprinting?
At a single gene locus, only one allele is active.
If the active gene is deleted or mutated, this can lead to a disease state.
Bohr effect
Deoxygenated hemoglobin accepts protons more readily than oxygenated Hg

This means that when pH is lower (i.e. increased [lactic acid] from excessive glycolysis due to exertion), the oxygen will pop off of Hg more readily.
2,3 bisphosphglycerate
Made from an intermediate of glycolysis

2,3-BPG decreases O2 affinity to Hg (induces oxygen to come off)

2,3 BPG shifts the O2 saturation curve (relative to partial pressure of oxygen) to the right

Interesting note: 2,3 BPG levels are higher in people who live at higher altitudes; likely require more oxygen to come off the RBC relative to the partial pressure
Sickle Cell Anemia mutation
Missense mutation (Glu --> Val) at AA position 6 of beta-chain

At low oxygen saturation, HbS proteins polymerize and 'sickle' inside RBC
methemoglobinemia
Ferrous heme (Fe2+) converts to Ferric heme (Fe3+) & loses ability to bind O2

can be from drugs or inherited conditions
beta-thalassemias
synthesis of beta-chain decreased or gone

excess alpha-chains form precipitate, which eventually kill the RBC

HbF and HbBart's build up in the system

Tx - regular transfusions, which can eventually lead to hemosiderosis
alpha-thalassemias
4 alpha genes; severity increases with number of mutations

(silent carrier, alpha-thalassemia trait, HgH, death)
hydroxyproline
post-translational modification found in collagen

important in stabilizing triple helix structure of collagen by minimizing H-bond formation
The 3 amino acids important to collagen formation
glycine - allows for tight helix wrapping

hydroxyproline - provides stabilization by minimizing H-bond formation

hydroxylysine - stabilize molecular structure; allow for carbohydrate attachment