جزاك الله خير على الشرح يا دكتور، الله يجعله علم ينتفع به ويثقل به ميزانك، أنا كل محاضرة بستفيد منها بدعيلك والله، الله يرضى عنك وينفع بك ويوفقك ويوفق أبناءك وبناتك وكل من تحب
The Triple Sugar Iron test is a microbiological test roughly named for its ability to test a microorganism's ability to ferment sugars and to produce hydrogen sulfide. It is often used in the selective identification of enteric bacteria including Salmonella and Shigella. ru-vid.com/video/%D0%B2%D0%B8%D0%B4%D0%B5%D0%BE-UQExR7nTO-k.html ru-vid.com/video/%D0%B2%D0%B8%D0%B4%D0%B5%D0%BE-mCav6y5p67c.html
السلام عليكم دكتور بارك الله في جهودك وحفظك الله انا طالب ماجستير وسؤال هو اي وسط افضل في زراعه السيدوموناس لاني استخدمت البروث وقال البعض استخدم الاكار وشكرا لك
Pseudomonas are not generally fastidious microorganisms. They can grow on very simple media like Kind Agar, for example, which contains a protein hydrolysate, magnesium chloride, potassium sulphate and agar. Analytical microbiology leverages a microbe’s unique biochemistry to aid in its identification. For example, selective Pseudomonas media use cetrimide, nalidixic acid, cephaloridine, penicillin G, pimaricin, malachite green and other inhibitory agents. The proteolytic activity, lipolytic activity, fluorescent pigment formation, nitrate utilisation, glutamate utilisation, hemolytic reaction and other biochemical reactions are used in the media for the identification and differentiation of Pseudomonas species.
دكتوووور محمد أرجوك اجبني على هذا السؤال : هل ال enterotoxin يحفز ال alternative complement pathway ??? اريد الحل بسرررعه لأن امتحاني قريب 😭 جزاك الله كل خير
+Inspiration Elham Mannose-binding lectin (MBL)-associated serine proteases (MASPs) are responsible for activation of the lectin complement path- way. Three types of MASPs (MASP-1, MASP-2, and MASP-3) are complexed with MBL and ficolins in serum. Although MASP-1 and MASP-2 are known to contribute to complement activation, the function of MASP-3 remains unclear. In this study, we in- vestigated the mechanism of MASP-3 activation and its substrate using the recombinant mouse MASP-3 (rMASP-3) and several different types of MASP-deficient mice. A proenzyme rMASP-3 was obtained that was not autoactivated during preparation. The recombinant enzyme was activated by incubation with Staphylococcus aureus in the presence of MBL-A, but not MBL-C. In vivo studies revealed the phagocytic activities of MASP-1/3-deficient mice and all MASPs (MASP-1/2/3)-deficient mice against S. aureus and bacterial clearance in these mice were lower than those in wild-type and MASP-2-deficient mice. Sera from all MASPs-deficient mice showed significantly lower C3 deposition activity on the bacteria compared with that of wild-type serum, and addition of rMASP-3 to the deficient serum restored C3 deposition. The low C3 deposition in sera from all MASPs-deficient mice was probably caused by the low level factor B activation that was ameliorated by the addition of rMASP-3. Furthermore, rMASP-3 directly activated factors B and D in vitro. These results suggested that MASP-3 complexed with MBL is converted to an active form by incubation with bacterial targets, and that activated MASP-3 triggered the initial activation step of the alternative complement pathway. Source: The Journal of Immunology, 2011, 187: 3751-3758.
