SUPPLEMENTAL Flashcards
THROWBACK KEY POINTS
how many microtubules comprise one microtubule?
what is unique about this structure?
13 protofilaments
hollow, cylindrical, straight tubule
formed from 9 microtubular triplets?
what is the arrangement
centriole
pinwheel, 3 microtubular fibrils A,B,C
these form basal bodies or kinetosome at cells surface?
why is this important?
centrioles
initiate formation of cilia, Micro Org Center
what is the shaft of the cilia?what is it formed from?
axoneme
basal body composed of 9 microtubular doublets surrounding a pair of microtubules in the center
what is example of thin filaments?
actin
what is example of thick filaments?
myosin
what are the examples of intermediate filaments?
cytokeratins vimentin desmin glial fibrillary acid protein neurofilaments
T/F, epithelia are vascular?
F, nonvascular
name this type of secretion:
apex of the cell lost as product? name an example?
apocrine, mammary glands
name this type of secretion:
entire cell dies and is secreted as product? example?
holocrine, sebaceous glands
name this type of secretion:
product is secreted via exocytosis
merocrine, most exocrine glands, pancreatic
types and examples of endocrine glands?
unicellular (diffuse neuroendocrine)
cord and clump
follicular (thyroid gland)
what are the types of junctional complexes?
occludens (tight)
adherens (desmosome)
gap junctions (nexus)
where are lysosomes synthesized?
golgi apparatus
what is unique about mitochondria in steroid secreting cells?
tubular cristae
this glut transporter is found in the muscle, heart and fat?
this is what type of transport?
glut 4
facilitated transporter
sodium dependent pump is what type of active transport?
secondary active transport
ABC transporter
intestina and renal glucose pump
intestinal and renal amino acid pump
calcium pumps in many cells
ATPases are what type of active transport?
primary
Na/K ATPase
SERCA pump
ATP Synthase
amino acids in proteins are in what configuration?
L-configuration
what amino is substituted in sickle cell disease?
glutamic acid is swapped for valine, so an acidic aa for a non polar aa
what are the uncharged polar amino acids?
serine threonine tyrosine asparagine cysteine glutamine
this amino acid is important in the active site of many enzymes?
phosphorylating a catabolic enzyme does what to its activity? what about to an anabolic enzyme?
serine
increases, decreases
this enzyme removes a phosphate?
this enzyme adds a phosphate?
this enzyme takes an ATP, removes the phosphate to add to another protein?
phosphatase
phosphorylase
protein kinase
what are the sites for attaching sugars?
asparagine
serine
threonine
these aa serve as condensation points for hydroxyapatite?
this aa cross links and is seen in collagen and fibrin clots?
proline and lysine
lysine
this is a secondary structure that refers to how neighboring alpha helices, beta sheets, and beta turns are oriented to each other?
motif
greek key
beta meander
the -OH group on what carbon is replaced by an -H on ribose or deoxyribose?
carbon 2
deoxyribose
this regulatory enzyme commits to ribose to be made into nucleotides or deoxynucleotides?
ribose phosphate pyrophosphokinase preps carbon 1 for synthesis of purine or pyrimidine
produces PRPP(5 phospho alpha, D ribose 1 pyrophosphate) from ribose 5 PO4
this is the precursor of both purine and pyrimidine nucleotides?
PRPP
key enzyme regulating how much PRPP becomes purine nucleotide?
amidophosphribosyl transferase
this is a glutamine analog which is antibacterial by blocking purine synthesis?
azaserine
what do purines make, IMP or UMP? what do pyrimidines make, IMP or UMP?
IMP
UMP
XMP to GMP via what enzyme?
GMP synthase
IMP to adenylosuccinate via what enzyme?
adenylosuccinate synthetase
key regulatory enzyme for DNA precursor synthesis?
ribonucleotide reductase
primary waste product of purine catabolism?
uric acid
this enzyme inhibits xanthine oxidase, used to treat gout?
allopurinol
if GPRTase is missing due to a genetic condition, this syndrome is developed which is characterized by aggression kidney stones renal failure and self mutilation
lesch nyhan syndrome
what are the pyrimidine catabolism breakdown products?
malonate
methyl malonate
what type of coiling compacts DNA?
negative supercoiling for less tension and ease of separation
T/F, histones are negative or positively charged?
positively charged
longest to shortest times of the phases of the cell cycle?
GI
S
G2
M, shortest*
this enzyme can only read in 1 direction and write in 1 direction?
DNA polymerase
reads 3-5
writes 5-3
T/F, can we use maternal lineage to track mitochondrial DNA?
T
most diverse least abundant RNA?
most abundant least diverse RNA?
more abundant than mRNA and the shortest of the RNAs?
mRNA
rRNA
tRNA
RNA polymerase directionality?
reads 3-5
writes 5-3
unlike DNA polymerase, no exonuclease
toxin produced by poisonous mushroom and called death cap?
alpha amanatin
what does RNA polymerase stabilize, sense or antisense strand and which one read?
sense strand
antisense strand
this enzyme breaks the 3’ bond to the amino acid on the aminoacyl tRNA at the P site and forms a peptide bond between the freed amino acid and the AA of the aminoacyl tRNA at the A site?
peptidyl transferase
