Immune globulin human (Human immunoglobulin) is a mixture of IgG1 and other antibodies derived from healthy human plasma and used to strengthen the body's natural defense system (immune system) to reduce the risk of infection in people with weakened immune systems. Human immunoglobulin is used as replacement therapy for inherited humoral immunodeficiency disorders, such as severe combined immunodeficiency syndrome, x-linked agammaglobulinemia, and Wiskott-Aldrich syndrome. Human immunoglobulin interacts with a number of different components of the immune system, including cytokines, complement, Fc receptors, and several immunocompetent cell surface molecules. Human immunoglobulin also acts on various effector cells of the immune system (B and T lymphocytes, dendritic cells, etc.) and regulates a wide range of genes. Human immune globulin competitively blocks gamma Fc receptors, preventing the binding and ingestion of phagocytes and inhibiting platelet depletion. Human immunoglobulin contains a number of different antibodies that prevent infection by attaching pathogenic microorganisms to the surface and facilitating their removal before they can infect cells. Antibodies remove pathogens by activating complement, agglutination or precipitation, blocking the pathogen receptor, “tagging” macrophages, or neutralizing the pathogen toxins. Serious adverse reactions are observed during intravenous treatment in clinical studies of aseptic meningitis. The most common adverse reactions were headache, fatigue, hyperthermia, nausea, chills, severity, pain in the limbs, diarrhea, migraine, dizziness, vomiting, cough, urticaria, asthma, sore throat and throat, rash, myalgia, itching, and cardiac murmur. During clinical trials of subcutaneous treatment, no serious adverse reactions were observed.

Cefixime, an antibiotic, is a third-generation cephalosporin like ceftriaxone and cefotaxime. Cefixime is highly stable in the presence of beta-lactamase enzymes. As a result, many organisms resistant to penicillins and some cephalosporins due to the presence of beta-lactamases, may be susceptible to cefixime. The antibacterial effect of cefixime results from inhibition of mucopeptide synthesis in the bacterial cell wall. Like all beta-lactam antibiotics, cefixime binds to specific penicillin-binding proteins (PBPs) located inside the bacterial cell wall, causing the inhibition of the third and last stage of bacterial cell wall synthesis. Cell lysis is then mediated by bacterial cell wall autolytic enzymes such as autolysins; it is possible that cefixime interferes with an autolysin inhibitor. Cefixime is sold under the brand name Suprax, indicated for the treatment of: Uncomplicated Urinary Tract Infections Otitis Media Pharyngitis and Tonsillitis Acute Exacerbations of Chronic Bronchitis Uncomplicated Gonorrhea (cervical/urethral)