Specific codes in ICD-10 are unique alphanumeric designations used to identify and categorize diseases, disorders, and conditions. They consist of 3-5 characters, including both letters and numbers, that provide a high level of detail and specificity.
Language | Translation |
---|---|
English | Chlamydial peritonitis |
French | Pรฉritonite ร Chlamydia (A74.8) |
Level | Code | Title | |
---|---|---|---|
1 | XI | Diseases of the digestive system | |
2 | K65-K67 | Diseases of peritoneum | |
3 | K67 | Disorders of peritoneum in infectious diseases classified elsewhere | |
4 | K67.0 | Chlamydial peritonitis |
Active Ingredient | Description | |
---|---|---|
Ceftolozane |
Ceftolozane belongs to the cephalosporin class of antimicrobials. Ceftolozane exerts bactericidal activity through binding to important penicillin-binding proteins (PBPs), resulting in inhibition of bacterial cell-wall synthesis and subsequent cell death. |
|
Minocycline |
Minocycline is a semi-synthetic derivative of tetracycline. Minocycline inhibits protein synthesis in susceptible bacteria. In common with other tetracyclines it is primarily bacteriostatic and has a similar spectrum of activity to other tetracyclines. |
|
Piperacillin |
Piperacillin is a broad-spectrum, semisynthetic penicillin. Piperacillin exerts bactericidal activity by inhibition of both septum and cell-wall synthesis. |
|
Spiramycin |
Antibacterial antibiotic belonging to the macrolides family. Spiramycin inhibits translocation by binding to bacterial 50S ribosomal subunits with an apparent 1:1 stoichiometry. This antibiotic is a potent inhibitor of the binding to the ribosome of both donor and acceptor substrates. Spiramycin induces rapid breakdown of polyribosomes, an effect which has formerly been interpreted as occurring by normal ribosomal run-off followed by an antibiotic-induced block at or shortly after initiation of a new peptide. |
|
Ticarcillin |
Ticarcillin disrupts bacterial cell wall development by inhibiting peptidoglycan synthesis and/or by interacting with penicillin-binding proteins. |