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1.
J Thorac Cardiovasc Surg ; 101(3): 488-94, 1991 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-1999943

RESUMO

Between June 1978 and June 1989, superficial or deep mediastinitis (or both) developed in only five (0.16%) of 3118 consecutive patients. All patients studied underwent cardiac procedures through a median sternotomy and survived more than 7 postoperative days. The surgical team disciplined itself to divide presternal soft tissues with a scalpel and used electrocautery for pinpoint hemostasis only. This 0.16% infection rate was statistically significantly lower than those in 28 previously published studies (Pearson's chi 2 test, p less than 0.05). Twenty-four predisposing factors were evaluated by Fisher's exact test. Among these only an operating time longer than 3 hours is related to sternotomy infections (p = 0.0208), and this effect was not a strong one. Statistical evidence strongly suggests that discriminate use of electrocautery is a major reason for the lowest median sternotomy infection rate reported to date.


Assuntos
Procedimentos Cirúrgicos Cardíacos , Eletrocoagulação , Mediastinite/epidemiologia , Esterno/cirurgia , Infecção da Ferida Cirúrgica/epidemiologia , Adulto , Idoso , Feminino , Humanos , Masculino , Mediastinite/prevenção & controle , Pessoa de Meia-Idade , Prevalência , Estudos Retrospectivos , Fatores de Risco , Infecção da Ferida Cirúrgica/prevenção & controle
2.
Biosci Biotechnol Biochem ; 62(4): 628-31, 1998.
Artigo em Inglês | MEDLINE | ID: mdl-27392551

RESUMO

Inulin fructotransferase (DFA III-producing) [EC 2.4.1.93] secreted from Bacillus sp. snu-7 was purified 60.3-fold with a yield of 11.6% from a culture supernatant by ammonium sulfate precipitation, preparative isoelectrofocusing, anion exchange chromatography and preparative polyacrylamide gel electrophoresis. The purified enzyme gave a single band on polyacrylamide gel electrophoresis. The molecular mass of the enzyme was estimated to be 62 kDa on SDS-polyacrylamide gel electrophoresis. The N-terminal amino acid sequence was found to be Ala-Asp-Gly-Gln-Asp-Gly-Ala-Pro-Leu-Asn-Gln-Val-Asn-Thr-Tyr-Asp. The optimal pH and temperature for the enzyme reaction were 6.0 and 40°C, respectively. The enzyme was stable with a pH range of 4.0 to 7.0 and at up to 60°C. As the production of di-D-fructose 1,2':2,3' dianhydride increased in the course of enzyme reaction, the Km of the purified enzyme was estimated to be 5.4 mM. One mM each of Cu(2+), Fe(2+) and Hg(2+) inhibited the enzyme activity strongly. Exhaustive enzymatic digestion of inulin produced 1-kestose, 1-nystose, and 1-F-fructofuranosylnystose as well as di-D-fructose 1,2':2,3' dianhydride.

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