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Clinical Isolates of Staphylococcus aureus Show Variation in β-Lactamase Production and Are More Susceptible to Antibiotics Conjugated with β-Lactamase Inhibitors

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Open Journal of Medical Microbiology 2016年第4期6卷 143-149页

作者： Uzal Umar Umar Ahmed Faruk Damoroem M. Tanko Mohammed B. Yerima Department for Biological Sciences Abubakar Tafawa Balewa University Bauchi Nigeria Department of Microbiology Federal University Dutse Dutse Nigeria

β-Lactam antibiotics are a cornerstone in the treatment of bacterial infections on account of its high therapeutic index and selective toxicity—they act by inhibiting the biosynthesis of peptidoglycan, a key component in bacterial cell wall. Ninety (90) clinical specimens obtained from the microbiology unit Specialist Hospital Bauchi were screened for S. aureus, positive isolates were examined for β-Lactamase expression by using two Penicillin G concentrations (5000 IU/ml and 25,000 IU/ml) in acidometric agar technique with phenol red as indicator, and the susceptibility pattern of the isolates to β-Lactam antibiotics was also determined. S. aureus prevalence of 31% (28/90) was obtained, of which 96% (27/28) of strains were β-Lactamase positive in the standard test, while 63% (17/27) were able to hydrolyze penicillin G concentration of 25,000 IU/ml (5X the concentration in the standard test), and a strain was found to be β-Lactamase negative. The resistance to five β-Lactams, ampicillin, cephalexin, amoxicillin, cloxacillin and flucloxaillin, were 100%, 96%, 89%, 74% and 56% respectively. When ampicillin and amoxicillin were conjugated to β-Lactamase inhibitors sulbactam and clavulanic acid respectively the resistance to ampicillin decreased to 21% and to amoxicillin to 15%. The antibiotic susceptibility profile revealed β-Lactamase elaboration to be the major mechanism of resistance to the β-Lactams. β-Lactam utilization as therapeutic option would thus require the search for sensitive irreversible β-Lactamase inhibitors for the β-Lactamase enzymes or agents to block the release of β-Lactamase by strains.

关键词： β-Lactamase Peptidoglycan transpeptidation Haemolysis Resistance Antibiotics

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A simple,economical method of converting gene expression products of insulin into recombinant insulin and its application

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Progress in Natural Science:Materials International 2003年第8期 38-42页

作者： ZHANG Zhou, CHEN Hui, TANG Yuehua and FENG Youmin(Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China)

A method, by which the gene expression product of recombinant single chain insulin can be converted into insulin by di-rectly digesting with trypsin, has been established. This method has been used in process of porcine insulin precursor (PIP), [B16Ala]PIP and [B26Ala]PIP into (desB30) insulin, (desB30) [B16Ala]insulin and (desB30) [B26Ala] insulin, respectively, and all of them re-tain full biological activity of that of their corresponding parent, recombinant human insulin, [B16Ala] insulin and [B26Ala] insulin. Theresults further demonstrate that the C-terminal residue of B chain is not necessary for insulin’s biological activity. Compared with themethod of transpeptidation, this method is simple, with a high yield, and avoids the use of organic reagents, and in comparison with thetrypsin/carboxypeptidase method, it omits the use of carboxylpeptidase. Besides, (desB30) [B16Ala] insulin and (desB30) [B26Ala] in-sulin still remained without self-association property as that of their parents, which demo

关键词： insulin (desB30)insulin trypsin/carboxylpeptidase transpeptidation monomeric insulin.

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