Purification and Characterisation of Extracellular Proteinase from Trichophyton rubrum / 대한의진균학회지
Korean Journal of Medical Mycology
;
: 51-58, 1997.
Artículo
en Coreano
| WPRIM
| ID: wpr-11268
ABSTRACT
BACKGROUND:
Trichophyton rubrum is the most common dermatophyte isolated from human and has ability to invade the tissues such as stratum comeum, nail and hair. The potential role of proteinases as virulence factors of F rMSrMm has been discussed at length.OBJECTIVE:
As a first step towards assessing its virulence role, we report on the purification and characterization of proteinase from T. rubrum isolate culture filtrates.METHODS:
An extracellular serine proteinase has been purified from culture filtrates of Trichophyton rubrum HP-9 by ultrafiltration, gel filtration chromatography, and affinity column chromatography. Azocoll and keratin azure were employed as the substrates of enzyme activities. Peak of proteolytic activity was analyzed by gelatin co-polymerized gel electrophoresis.RESULTS:
The molecular weight of the purified enzyme was approximately exhibited to 14.0 kDa on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The optimum pH and molality of 14.0 kDa proteinase activity was 6.0 and 100mM, respectively. The activity was inhibited by serine proteinase inhibitor, phenylmethylsulfonyl fluoride (PMSF). The proteinase degraded gelatin, collagen type VI, and keratin from human epidermis but not hemoglobin.CONCLUSION:
The 14,000 Mr extracellular serine proteinase purified from T. rubrum NP-9 culture filtrates has neutral pH optimum 6.0 and activities against gelatin, collagen type VI, and keratin.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Péptido Hidrolasas
/
Fluoruro de Fenilmetilsulfonilo
/
Dodecil Sulfato de Sodio
/
Trichophyton
/
Virulencia
/
Ultrafiltración
/
Cromatografía
/
Cromatografía en Gel
/
Colágeno Tipo VI
/
Factores de Virulencia
Límite:
Humanos
Idioma:
Coreano
Revista:
Korean Journal of Medical Mycology
Año:
1997
Tipo del documento:
Artículo
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