Busy. Please wait.
Log in with Clever

show password
Forgot Password?

Don't have an account?  Sign up 
Sign up using Clever

Username is available taken
show password

Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
Your email address is only used to allow you to reset your password. See our Privacy Policy and Terms of Service.

Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
Didn't know it?
click below
Knew it?
click below
Don't Know
Remaining cards (0)
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

Biochem Test 1


produced in response to invasion by foreign compounds (antigens) Antibodies
Antibody binding to an antigen initiates a process that eliminates the foreign substance
Antigens may have several antigenic determinant regions in them called epitopes
in what cases do antibodies recognize own structure? rheumatoid arthritis, type 1 diabetes
Immunoglobulin molecules consist of four polypeptide chains, two identical copies of two different chains, designated L and H.
four chains are covalently interconnected by disulfide bonds
gives the molecule flexibility upon antigen binding and where heavy chains are interconnected hinge region
the most common immunoglobulin IgG
Why IgG 3D struct instead of quaternary? b/c quaternary structs require noncovalent bonds, and IgG has covalent bonds (the disulfide bonds that hold the L&H together)
how many domains of the constant C region are on the H chain? L chain? 3 - H 1 - L
N-terminal sequences are variable (V) regions and are designated VH and VL
Within the V regions, certain segments are hypervariable, called complementarity-determining regions (CDRs)
form the antigen binding sites complementarity-determining regions (CDRs)
variable regions give the antibody its specificity
N terminal half of the L chains and the N terminal quarter of the H chains are highly variable between different antibody molecules
C-terminal three quarters of the H chains and the C terminal half of the L chains are homologous in sequence with the other H or L chains of the same class of antibodies
these regions have a homologous primary structure constant (C) regions
these regions determine the antibody class CH regions
binding site for complement proteins CH regions
site necessary for antibodies to cross the placental membrane CH regions
what carries specificity in the hypervariable region of variable domain in L and H? random coils
each chain of an antibody molecule has a repeating pattern of structure, called domains
how many domains in H-chain? L-chain? H: four domains, VH region and three CH regions L: two domains, VL region and CL region
Each domain folds into a structure built by antiparallel β-pleated sheets
domain folds built by antiparallel β strands generate a motif known as all-beta immunoglobulin fold
each domain is stabilized and cross-linked by s-s and random coils
Ig is modified by carbohydrates
what does protein A do? precipitate Antibody to detect and quantify
what's Clq? complement cascade that plays role in eliminating Ag
describe series from antigen to complement 1) Ag binds Ab 2) exposes C1, allows C1 to bind Ab 3) activates macrophages
function of Antibodies? recognition and binding of foreign molecules and the initiation of their removal
When antibodies bind to antigens, small changes in conformation occur where? CDRs (complement determining regions)
Conformation change in CDR (located in V-region) caused by Ag binding to Ab, cause conformation change where? C-terminal region
when c-terminal region changes conformation, what happens next? exposes complement binding site at Fc region and allow binding of C1 complex, activates complement system, and lyses cell membrane
complement proteins are precursors of proteolytic enzymes
The major role of the complement system is to generate opsonins
proteins that stimulate phagocytosis by neutrophils and macrophages opsonins
major opsonin that bind to specific receptors on the macrophage cell surface C3b
Patients with inherited deficiency of C3 (an opsonin) are subject to repeated bacterial infections
Characteristics of each class are due to differences in heavy chains.
H chains γ occur in which Ig? IgG
H chains α occur in which Ig? IgA
H chains δ occur in which Ig? IgD
H chains ε occur in which Ig? IgE
H chains μ occur in which Ig? IgM
how many classes of H chains are there? five
Two types of L chains are? lambda (λ) and kappa (κ)
which Ig classes are most prominent in immune response in blood? IgG and IgM
these Ig classes are monomers (LH)2 IgAs, IgDs, IgEs and IgGs
Which Ig class is in seromucosal secretions are covalently linked dimeric structures ((LH)2)2 IgA
what keeps dimers and pentamers in IgA and IgM together? J-chain
IgA's seromucosal secretions are found in? Mother's milk, saliva, eyes brochial, nasal, intestinal secretions
function of seromucosal secretions? fight Ag before they get through epithelial cells and body
This class of Ig are pentamers ((LH)2)5 IgMs
Biosynthesis of a specific IgG in significant levels takes about how many days after exposure to a new antigen? 10 days
Which Ig class is made first and faster and serve as the first line of defense until IgGs are made IgMs
How many weeks after initial Ag contact is IgG synthesized? 2 weeks
They are the initial defense against viral and bacterial pathogens prior to entry into plasma or internal space IgA class of immunoglobulins
neutralize viruses, toxins and block bacterial adherence on mucosal surfaces IgAs
They are the first antibodies elicited in significant quantities on exposure to foreign antigen IgM class
This class of Ig found in many external secretions but at lower levels than IgA IgM
this Ig class promotes phagocytosis of microorganisms by macrophages and polymorphonuclear leukocytes, and is a potent activator of the complement system IgM
what is order of Ig classes from most concentrated in plasma to least? IgG, IgA, IgM, IgD, IgE
This is the only antibody that is able to cross the placenta IgG
this class can secrete to breast milk, thus provides immunity to newborns IgG
It serves as antigen receptor on lymphocytes and participates in their activation. IgD
mediates immediate hypersensitivity reactions, thus plays a role in allergic responses such as anaphylactic shock, hay fever and asthma. IgE
is also considered an anti-parasite antibody IgE
selective IgA deficiency results in recurrent infection of sinus and the respiratory tract
An immunizing vaccine can consist of killed bacterial cells, inactivated viruses, killed parasites, a nonvirulent form of live bacterium related to a virulent bacterium or denatured bacterial toxin or recombinant protein
Antigens not only cause differentiation of lymphoid cells so they produce antibody but also cause differentiation of some of the cells into memory cells.
they do not secrete antibody but place antibody on their outer surface and serve as radar Memory cells
reduces the time needed for defense and increases the concentration of antigen specific antibody memory cells
what's Multiple myeloma uncontrolled proliferation of plasma cells and the synthesis of a homogenous gamma globulin, called M-protein
Only one type of immunoglobulin is produced with one type of light chain is overproduced monoclonal gammopathies
monoclonal gammopathies: plasma and urine electrophoreses show typical single peak in the gamma globulin
a doublet of a kappa or lambda light chain Bence- Jones protein
light chain secreted in the urine Multiple myeloma patient is Bence- Jones protein (doublet of a kappa or lambda light chain)
what are the clinical manifestations of multiple myeloma? Bone fractures, Bleeding, Chronic renal failure, anemia, granulocytopenia and thrombocytopenia
Created by: rosejames05
Popular Biochemistry sets




Use these flashcards to help memorize information. Look at the large card and try to recall what is on the other side. Then click the card to flip it. If you knew the answer, click the green Know box. Otherwise, click the red Don't know box.

When you've placed seven or more cards in the Don't know box, click "retry" to try those cards again.

If you've accidentally put the card in the wrong box, just click on the card to take it out of the box.

You can also use your keyboard to move the cards as follows:

If you are logged in to your account, this website will remember which cards you know and don't know so that they are in the same box the next time you log in.

When you need a break, try one of the other activities listed below the flashcards like Matching, Snowman, or Hungry Bug. Although it may feel like you're playing a game, your brain is still making more connections with the information to help you out.

To see how well you know the information, try the Quiz or Test activity.

Pass complete!
"Know" box contains:
Time elapsed:
restart all cards