[LEC/LAB] Antibodies Flashcards
NUMBER OF POLYPEPTIDE UNITS
4
NUMBER OF AMINO ACIDS ON THE HEAVY CHAINS
450
NUMBER OF AMINO ACIDS ON THE LIGHT CHAINS
220
IMMUNOGLOBULIN CLASSES ON THE HEAVY CHAINS
DELTA
ALPHA
GAMMA
EPSILON
MU
IMMUNOGLOBULIN CLASSES ON THE LIGHT CHAINS
KAPPA
LAMBDA
WHICH IMMUNOGLOBULIN CLASSES ARE PRESENT ON ALL LIGHT CHAINS
KAPPA
LAMBDA
FORMER NAME OF IMMUNOGLOBULINS
GAMMA GLOBULINS
WHY IS KAPPA MORE THAN LAMBDA IN THE LIGHT CHAIN
DUE TO GENETIC REARRANGEMENT
LAMBDA STEMS FROM KAPPA
HOLDS LIGHT CHAIN TO HEAVY CHAIN
DISULFIDE BONDS
CONSISTS OF 1 LIGHT CHAIN AND 1/2 HEAVY CHAIN
FAB FRAGMENT
HOW MANY FRAGMENTS MAKE UP 1 AG BINDING SITE
2 FAB FRAGMENTS
MEANING OF FAB
FRAGMENT ANTIGEN BINDING
MEANING OF FC
FRAGMENT CRYSTALLINE
CARBOXY TERMINAL END HALVES OF THE TWO HEAVY CHAINS
FC FRAGMENT
PORTION OF THE ANTIBODY THAT HAS NO AG-BINDING ABILITY
FC PORTION
IG PART THAT IS RESPONSIBLE FOR DETERMINING THE TYPE OF CLASS AND AG-AB REACTION THAT OCCURS
CONSTANT REGION
IG PART THAT DIFFERS ANTIBODY CLASSES FROM EACH OTHER
CONSTANT REGION OF THE HEAVY CHAIN
AMINO TERMINAL END OF THE IG
VARIABLE REGION
PART OF THE IG WHERE AMINO ACID SEQUENCE VARIES
VARIABLE REGION
PART OF THE IG THAT IS RESPONSIBLE FOR ITS SPECIFICITY
VARIABLE REGION
REFERS TO THE NUMBER OF BINDING SITES
VALENCE
FLEXIBLE PORTION OF THE HEAVY CHAIN
HINGE REGION
LOCATION OF THE HINGE REGION
BETWEEN THE FIRST AND SECOND CONSTANT REGIONS
GLYCOPROTEIN THAT SERVES TO LINK IG MONOMERS TOGETHER
J CHAIN
IMMUNOGLOBULINS THAT HAVE A J CHAIN
IGA
IGM
PH AT WHICH SERUM PROTEINS CAN BE SEPARATED
PH 8.6
SLOWEST MOVING PROTEIN
IG
REGION IN WHICH IMMUUNOGLOBULINS APPEAR IN AN ELECTROPHORETIC SET UP
GAMMA BAND
MAIN HUMORAL ELEMENT OF THE ADAPTIVE IMMUNE RESPONSE
IG
FIVE MAJOR CLASSES OF IG
GMADE
HOW MANY VARIABLE REGIONS AND CONSTANT REGIONS DOES A CHAIN HAVE
1 VARIABLE REGION
1 OR MORE CONSTANT REGIONS
SCIENTISTS WHO WORKED ON IGGs
EDELMAN
PORTER
SOLUTION EDELMAN USED TO UNFOLD THE IGG MOLECULE
7M UREA
SOLUTION USED TO BREAK DOWN SULFHYDRYL BONDS
MERCAPTOETHANOL
ENZYME USED TO CLEAVE IGG INTO THREE PIECES
PAPAIN
METHOD USED BY PORTER TO SEPARATE IGG
CARBOXYMETHYL CELLULOSE ION EXCHANGE CHROMATOGRAPHY
CRYSTALLIZATION OF THE FC FRAGMENT OCCURED AT WHAT TEMPERATURE
4C
EFFECTOR FUNCTIONS OF THE FC PORTION
OPSONIZATION
COMPLEMENT FIXATION
ENZYME USED TO CLEAVE IGG AT THE CARBOXY TERMINAL SIDE OF THE INTERCHAIN DISULFIDE BONDS
PAPAIN
DIFFERENCE BETWEEN FC AND FC’
FC1 DISINTEGRATES INTO SEVERAL SMALLER PIECE WHEN CLEAVED
PROTEIN FOUND IN THE URINE OF PATIENTS WITH THIS CLINICAL CONDITION
BENCE JONES PROTEINS
CELLS THAT SECRETE THE BENCE JONES PROTEINS
MALIGNANT PLASMA CELLS
BEHAVIOR OF BENCE JONES PROTEINS WHEN HEATED
60C — PRECIPITATE FROM URINE
80C — REDISSOLVE
PERCENTAGE OF KAPPA CHAINS
60%
[TRUE OR FALSE]
THERE ARE NO FUNCTIONAL DIFFERENCES BETWEEN KAPPA AND LAMBDA CHAINS
TRUE
CHAINS THAT ARE FOUND N ALL FIVE CLASSES OF IG
KAPPA
LAMBDA
MINOR VARIATIONS OF IGG SEQUENCES PRESENT IN SOME INDIVIDUALS BUT NOT OTHERS
ALLOTYPES
UNIQUE AMINO ACID SEQUENCE THAT IS PRESENT ON ALL IG CLASSES IN A GIVEN SPECIES
ISOTYPE
GENETIC MARKERS FOUND ON THE CONSTANT REGION
ALLOTYPES
VARIABLE PORTIONS OF EACH CHAIN THAT ARE UNIQUE TO A SPECIFIC AB MOLECULE
IDIOTYPE
PART OF THE IG THAT CONTAINS THE IDIOTYPE
AMINO TERMINAL ENDS
OF H AND L CHAINS
THE AG RECOGNITION UNIT IS COMPOSED OF WHICH PARTS OF THE IG
AMINO TERMINAL ENDS OF
THE L AND H CHAINS
PROTEIN THAT ALLOWS THE HINGE REGION TO BE FLEXIBLE
PROLINE
IG CLASSES WITH AND WITHOUT THE HINGE REGION
WITH — GDA
WITHOUT — ME
FUNCTIONS OF THE CARBOHYDRATE PORTION
INCREASE SOLUBILITY
PROVIDE PROTECTION AGAINST DEGRADATION
ENHANCE FUNCTIONAL ACTIVITY OF THE FC DOMAINS
REGION THAT IS DIRECTLY IN CONTACT WITH THE AG AND CAN MUTATE TO PRODUCE MORE SPECIFIC AND DIVERSE RESPONSES
HYPERVARIABLE REGION
PREDOMINANT IG IN HUMANS
IGG
(70-75%)
IG WITH THE LONGEST HALF LIFE
IGG
23 DAYS
SUBCLASSES OF IGG
IGG1
IGG2
IGG3
IGG4
DIFFERENTIATING CHARACTERISTIC OF IGG SUBCLASSES
NUMBER AND POSITION OF DISULFIDE BRIDGES
WHAT AFFECTS THE ABILITY TO REACH FOR AN AG AND INITIATE BIOLOGICAL FUNCTIONS
VARIABILITY IN THE HINGE REGION
IGG SUBCLASS WITH THE LARGEST HINGE REGION
IGG3
3 > 1 > 2 > 4
IGG SUBCLASS WITH THE LARGEST NUMBER OF INTERCHAIN DISULFIDE BONDS
IGG3
MOST EFFICIENT IGG SUBCLASS AT BINDING COMPLEMENT
IGG3
3>1>2>4
IGG SUBCLASSES WITH SHORTER HINGE REGIONS AND THEIR EFFECTS ON COMPLEMENT ACTIVATION
IGG4
IGG2
MAKES THE POOR MEDIATORS OF COMPLEMENT ACTIVATION
IGG SIBCLASS THAT CANNOT CROSS THE PLACENTA
IGG2
IG THAT PROVIDES IMMUNITY FOR THE NEWBORN AND WHY
IGG
Only IgG that can cross the placenta
IG THAT FIXES COMPLEMENT
IGG
IG THAT COATS ANTIGEN FOR ENHANCED PHAGOCYTOSIS
IGG
Opsonization
WHAT IS OPSONIZATION
COATING OF AN ANTIGEN FOR ENHANCED PHAGOCYTOSIS
IG THAT NEUTRALIZES TOXINS AND VIRUSES
IGG
IG THAT IS BEST AT PRECIPITATION REACTIONS
IGG
IGG SUBCLASS THAT RESPOND TO PROTEIN AG
IGG1
IGG3
IGG SUBCLASSES THAT RESPOND TO POLYSACCHARIDE AG
IGG2
IGG4
CELLS THAT HAVE RECEPTORS SPECIFIC FOR IGG
MACROPHAGES
MONOCYTES
NEUTROPHILS
IGG SUBCLASS THAT IS GOOD AT INITIATING PHAGOCYTOSIS
IGG3
EFFECT OF HAVING A HIGH DIFFUSION COEFFICIENT
ABLE TO ENTER EXTRAVASCULAR SPACES MORE READILY
WHY IS IGG BETTER AT PRECIPITATION REACTIONS
BECAUSE PRECIPITATION INVOLVES SMALL SOLUBLE PARTICLES
IG CLASS KNOWN AS A MACROGLOBULIN
IGM
HALF LIFE OF IGM
ABOUT 6 DAYS
PERCENTAGE OF IGM
5% TO 10%
SOLUTION THAT DISSOCIATES IGM
MERCAPTOETHANOL
IGM FORM FOUND IN SERUM
PENTAMER
IGM FORM FOUND ON THE SURFACE OF B CELLS
MONOMER
LINKAGE POINTS FOR DISULFIDE BONDS BETWEEN TWO ADJACENT MONOMERS
J CHAIN
HOW DOES THE J CHAIN INITIATW POLYMERIZATION
BINDING FC SULFHYDRYL GROUPS SO THAT CROSS LINKING CAN OCCUR
WHAT FACILITATES SECRETION AT MUCOSAL SURFACES
J CHAIN
HOW MANY J CHAINS ARE PRESENT PER PENTAMER
ONE
STARLIKE SHAPE
IGM
WHAT PROPERTY OF IGM MAKES UP FOR THEIR POOR AFFINITIES FOR AG
HIGH VALENCY
MAIN LOCATION OF IGM
INTRAVASCULAR POOL
NOT IN OTHER BODY FLUIDS OR TISSUES
PRIMARY RESPONSE AB
IGM
FIRST IG TO APPEAR AFTER ANTIGENIC STIMULATION
IGM
FIRST IG TO APPEAR IN A MATURING INFANT
IGM
IG THAT IS SYNTHESIZED ONLY WHILE AG IS PRESENT
IGM
WHY IS IGM SYNTHESIZED ONLY WHEN AG IS PRESENT
NO MEMORY CELLS FOR IGM
PRESENCE OF THIS AB INDICATES A PRIMARY EXPOSURE TO AG
IGM
PHENOMENON CHARACTERIZED BY:
LONG LAG PHASE
SLOW INCREASE IN AB
SHORT-LIVED RESPONSE
PRIMARY RESPONSE
PHENOMENON CHARACTERIZED BY:
LARGER NUMBER OF AG-SPECIFIC MEMORY T AND B CELLS
SECONDARY RESPONSE
IG USED IN COMPLEMENT FIXATION
IGM
IG BEST AT AGGLUTINATION AND WHY
IGM
HIGH VALENCY
IG USED IN OPSONIZATION
IGM
IG USED TO NEUTRALIZE TOXINS
IGM
MOST EFFICIENT IG AT ACTIVATING THE COMPLEMENT PATHWAY
IGM
IG THAT SERVES AS A SURFACE RECEPTOR FOR AG
IGM
CHAINS THAT APPEAR FIRST IN THE CYTOPLASM OF THE PRE-B CELL
MU CHAINS
IG THAT CLASSIFIES LYMPHOCYTES AS IMMATURE B CELLS
IGM
CAN IGs HAVE ODD NUMBERED VALENCES
NO
MOST PRIMITIVE IG
IGM
FIRST IG TO APPEAR IN PHYLOGENY AND LAST TO LEAVE IN SENSENCE
IGM
IG THAT MIGRATES BETWEEN THE BETA AND GAMMA REGIONS
IGA
SUBCLASSES OF IGA
IGA1
IGA2
IGA SUBCLASS THAT IS MORE RESISTANT TO BACTERIAL PROTEINASES
IGA2
PREDOMINANT IGA SUBCLASS IN SECRETIONS AT MUCOSAL SURFACES
IGA2
PREDOMINANT IGA SUBCLASS IN SERUM
IGA1
ANTI INFLAMMATORY IG
IGA
DOWNREGULATES PHAGOCYTOSIS, CHEMOTAXIS, BACTERICIDAL ACTIVITY, AND CYTOKINE RELEASE
IGA
WHAT DOMAINS DOES IGA2 PREDOMINANTLY PATROL AND WHY
MUCOSAL SURFACES
BECAUSE THEY ARE MAJOR ENTRY POINTS FOR PATHOGENS
IG WITH A SECRETORY COMPONENT
IGA
DESCRIBE THE FORMATION OF SECRETORY IGA
IGA IS SECRETED AS A DIMER FROM PLASMA CELLS
IGA IS CAPTURED BY RECEPTORS ON EPITHELIAL CELLS
(RECEPTOR IS SC)
SC BINDS WITH IGA AND EXITS THE CELL AS ONE
PROCESS OF TAKING THE IGA AND SC PRECURSOR INTO THE CELL AND RELEASING IT TO THE OPPOSITE SURFACE
TRANSCYTOSIS
MAIN FUNCTION OF IGA
PATROL MUCOSAL SURFACES AND ACT AS THE FIRST LINE OF DEFENSE
IG FOUND IN BREASTMILK
IGA
ADVANTAGE OF IGA NOT BEING ABLE TO ACTIVATE COMPLEMENT
MINIMIZATION OF TISSUE DAMAGE
LACK OF COMPLEMENT ASSISTS IN CLEARING THE ANTIGEN WITHOUT TRIGGERING AN INFLAMMATORY RESPONSE
BINDING OF IGA TO NEUTROPHILS, MONOCYTES, AND MACROPHAGES TRIGGERS WHAT REACTION
RESPIRATORY BURST
DEGRANULATION
DISCOVERY OF IGD WAS IN A PATIENT WITH WHAT CLINICAL CONDITION
MULTIPLE MYELOMA
EXTREMELY SCARCE IG IN SERUM
IGE
HALF LIFE OF IGD
1 TO 3 DAYS
WHAT KIND OF CELLS ARE MOST IGD FOUND ON
IMMUNOCOMPETENT BUT UNSTIMULATED
B LYMPHOCYTES
SECOND IG TO APPEAR IN B CELL ACTIVATION
IGA
CHARACTERISTIC OF IGD THAT MAKES IT AN IDEAL EARLY RESPONDER TO AG
HIGH LEVEL OF SURFACE EXPRESSION
IG MOST SUSCEPTIBLE TO PROTEOLYSIS AND WHY
IGD
UNUSUALLY LONG HINGE REGION
IG THAT HAS THE ABILITY TO ACTIVATE MAST CELLS AND BASOPHILS
IGE
LEAST ABUNDANT IG
IGE
MOST HEAT LABILE IG
IGE
HEAT STABILITY TEST CONDITIONS OF IGE
56C FOR 30 MINS TO 3 HRS
IG THAT DOES NOT PARTICIPATE IN COMPLEMENT FIXATION, AGGLUTINATION, OPSONIZATION
IGE
CELL FOUND MAINLY IN THE SKIN AND LINING OF RESPIRATORY TRACTS
MAST CELLS
IG THAT BINDS STRONGLY TO THE RECEPTORS ON MAST CELLS AND BASOPHILS
IGE
PROTEINS THAT MAKE CELLS POROUS FOR GRANZYMES TO ENTER AND PROMOTE APOPTOSIS
PERFORINS
IG THAT IS ANTIPARASITIC
IGE
[ANTIBODY DIVERSITY THEORY]
TEMPLATE THEORY
BREINT HAROWITZ
AG WILL BE THE MOULD OR PATTERN FOR AB PRODUCTION
[ANTIBODY DIVERSITY THEORY]
SIDE CHAIN
PAUL EHRLICH
B CELLS CONTAIN ALL AB TO AG
BODY WILL CHOSE WHICH AB TO REPRODUCE
[ANTIBODY DIVERSITY THEORY]
INSTRUCTIONAL HYPOTHESIS
TEMPLATE THEORY
[ANTIBODY DIVERSITY THEORY]
FUNDAMENTAL BASIS OF LYMPHOCYTE ACTIVATION
CLONAL SELECTION THEORY
[ANTIBODY DIVERSITY THEORY]
CLONAL SELECTION THEORY
B CELL ONLY HAS ONE AG
BODY WILL DUPLICATE THE CHOSEN B CELL
MEMORY B CELLS WILL BE FORMED
GENE THAT EXPRESSES WHAT AB TO CREATE
VDJ GENE
EXPLAIN HOW CLASS SWITCHING WORKS
T DEPENDENT AG WILL SWITCH
START WITH IGM
SWITCH TO THE CLASS THAT IS AFTER IGM
RECOMBINATION EVENT WILL EXPRESS NEW CLASSES OF HEAVY CHAINS
PLASMA CELL + MYELOMA CELL
HYBRIDOMA
METHOD THAT APPLIES HYBRIDOMA TECHNOLOGY WITH SPLEEN CELLS FROM A MOUSE
MONOCLONAL AB PRODUCTION
SPLEEN CELLS ARE COMBINED WITH MYELOMA CELLS IN THE PRESENCE OF
POLYETHYLENE GLYCOL
PEG
CULTURE USED IN MONOCLONAL ANTIBODY PRODUCTION TECHNIQUE
HAT MEDIUM
HYPOXANTHINE
AMINOPTERIN
THYMIDINE
