Chemical modification of $\alpha$-galactosidase from Thermus thermophilus HB8
Küçük Resim Yok
Tarih
1998
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
Thermus thermophilus HB8'den saflaştırılan $\alpha$-galaktosidazın inhibisyonu, enzimin histidin, sistein, triptafan ve serbest karboksil grubu içeren aminoasitlerinin kimyasal modifikasyonu ile incelendi, $\alpha$-galaktosidazın N-bromosüksinamid ve Woodward reaktifleriyle muamele edilmesi sonucunda enzimin tersinir olarak inhibe edildiğinin belirlenmesi, enzim aktif merkezinde veya yakınında triptofan ile aspartik ve glutamik asitlerin varlığının bir göstergesidir. Buna karşılık $\alpha$-galaktosidazın dietilpirokarbonat ve Ellman reaktifleriyle muamelesi sonrasında enzim aktivitesinin geri dönüşümsüz kaybı, histidin ve sisteinin aksiyon mekanizmasında zorunlu olarak görev almalarına karşın aktif merkezde yer almadıklarını gösterdi.
The inhibition of $\alpha$-galactosidase, which was purified from Thermus thermophilus HB8 was studied by chemical modification of its ; histidine, cysteine, tryptophan and free carboxyl group containing amino acid residues. The treatment with N-bromosuccinimide and Woodward's Reagent K indicated that the enzyme was inhibited reversibly, suggesting tryptophan -and aspartic/glutamic acids are at or near the active site. In contrast the treatment with diethylpyrocarbonate and Ellman's reagent resulted in irreversible loss of the enzyme activity, implying that histidine and cysteine are essential for the mechanism of action, but not located at the active site.
The inhibition of $\alpha$-galactosidase, which was purified from Thermus thermophilus HB8 was studied by chemical modification of its ; histidine, cysteine, tryptophan and free carboxyl group containing amino acid residues. The treatment with N-bromosuccinimide and Woodward's Reagent K indicated that the enzyme was inhibited reversibly, suggesting tryptophan -and aspartic/glutamic acids are at or near the active site. In contrast the treatment with diethylpyrocarbonate and Ellman's reagent resulted in irreversible loss of the enzyme activity, implying that histidine and cysteine are essential for the mechanism of action, but not located at the active site.
Açıklama
Anahtar Kelimeler
Mühendislik, Ortak Disiplinler
Kaynak
Ege University Journal of The Faculty of Science
WoS Q Değeri
Scopus Q Değeri
Cilt
21
Sayı
1
