The nine multidrug resistance proteins (MRPs) represent the major part of the 12 members of the MRP/CFTR subfamily belonging to the 48 human ATP-binding cassette (ABC) transporters. Cloning, functional characterization, and cellular localization of most MRP subfamily members have identified them as ATP-dependent efflux pumps with broad substrate specificity for the transport of endogenous and xenobiotic anionic substances localized in cellular plasma membranes. Multidrug resistance protein (MRP) is a broad specificity, primary active transporter of organic anion conjugates that confers a multidrug resistance phenotype when transfected into drug-sensitive cells. The protein was the first example of a subgroup of the ATP-binding cassette superfamily whose members have three membrane-spanning domains (MSDs) and two nucleotide binding domains.

Correct Option: A

The nine multidrug resistance proteins (MRPs) represent the major part of the 12 members of the MRP/CFTR subfamily belonging to the 48 human ATP-binding cassette (ABC) transporters. Cloning, functional characterization, and cellular localization of most MRP subfamily members have identified them as ATP-dependent efflux pumps with broad substrate specificity for the transport of endogenous and xenobiotic anionic substances localized in cellular plasma membranes. Multidrug resistance protein (MRP) is a broad specificity, primary active transporter of organic anion conjugates that confers a multidrug resistance phenotype when transfected into drug-sensitive cells. The protein was the first example of a subgroup of the ATP-binding cassette superfamily whose members have three membrane-spanning domains (MSDs) and two nucleotide binding domains.

Sulfonamides were the first drugs acting selectively on bacteria which could be used systemically. Today they are infrequently used, in part due to widespread resistance. The target of sulfonamides, and the basis for their selectivity, is the enzyme dihydropteroate synthase (DHPS) in the folic acid pathway. Quinolones are molecules structurally derived from the heterocyclic aromatic compound quinoline, the name of which originated from the oily substance obtained after the alkaline distillation of quinine. They have antimicrobial activity because of their action against the topoisomerase enzyme. Erythromycin is a macrolide antibiotic used to treat bacterial infections. By binding to the 50s subunit of the bacterial 70s rRNA complex, protein synthesis and subsequent structure and function processes critical for life or replication are inhibited. They prevent peptidoglycan synthesis. Cephalosporins are medicines that kill bacteria or prevent their growth. Cephalosporins disrupt the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity. The final transpeptidation step in the synthesis of the peptidoglycan is facilitated by transpeptidases known as penicillin-binding proteins (PBPs). PBPs bind to the D-Ala-D-Ala at the end of muropeptides (peptidoglycan precursors) to crosslink the peptidoglycan. Beta-lactam antibiotics mimic the D-Ala-D-Ala site, thereby competitively inhibiting PBP crosslinking of peptidoglycan.

Correct Option: D

Sulfonamides were the first drugs acting selectively on bacteria which could be used systemically. Today they are infrequently used, in part due to widespread resistance. The target of sulfonamides, and the basis for their selectivity, is the enzyme dihydropteroate synthase (DHPS) in the folic acid pathway. Quinolones are molecules structurally derived from the heterocyclic aromatic compound quinoline, the name of which originated from the oily substance obtained after the alkaline distillation of quinine. They have antimicrobial activity because of their action against the topoisomerase enzyme. Erythromycin is a macrolide antibiotic used to treat bacterial infections. By binding to the 50s subunit of the bacterial 70s rRNA complex, protein synthesis and subsequent structure and function processes critical for life or replication are inhibited. They prevent peptidoglycan synthesis. Cephalosporins are medicines that kill bacteria or prevent their growth. Cephalosporins disrupt the synthesis of the peptidoglycan layer of bacterial cell walls. The peptidoglycan layer is important for cell wall structural integrity. The final transpeptidation step in the synthesis of the peptidoglycan is facilitated by transpeptidases known as penicillin-binding proteins (PBPs). PBPs bind to the D-Ala-D-Ala at the end of muropeptides (peptidoglycan precursors) to crosslink the peptidoglycan. Beta-lactam antibiotics mimic the D-Ala-D-Ala site, thereby competitively inhibiting PBP crosslinking of peptidoglycan.

A humanized chain is a chain in which the complementarity determining regions (CDR) of the variable domains are foreign (originating from one species other than human, or synthetic) whereas the remaining chain is of human origin.

Correct Option: D

A humanized chain is a chain in which the complementarity determining regions (CDR) of the variable domains are foreign (originating from one species other than human, or synthetic) whereas the remaining chain is of human origin.

Heat-inactivation (heating to 56°C for 30 minutes) of serum is done to inactivate complement, a group of proteins present in sera that are part of the immune response.

Correct Option: C

Heat-inactivation (heating to 56°C for 30 minutes) of serum is done to inactivate complement, a group of proteins present in sera that are part of the immune response.

A nude mouse is a laboratory mouse from a strain with a genetic mutation that causes a deteriorated or absent thymus, resulting in an inhibited immune system due to a greatly reduced number of T cells.

Correct Option: B

A nude mouse is a laboratory mouse from a strain with a genetic mutation that causes a deteriorated or absent thymus, resulting in an inhibited immune system due to a greatly reduced number of T cells.