Purification and Characterization of Cysteine-43  Mutant Citrate Synthase from Thermoplasma  acidophilum

İpek ERDURAN

Makale detayları

Purification and Characterization of Cysteine-43 Mutant Citrate Synthase from Thermoplasma acidophilum

Yazarlar:

İpek ERDURAN

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 1999 Vol.23 Issue 4, pp.423-432

Belge Tipi:

Makale

Yayın Tarihi:

3/1999

Belge Dili:

Türkçe

Document ID (Org No.):

2000814193

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152

Anahtar kelimeler:

Özet:

 

Two cysteine residues were introduced to selected positions (Serine-309 and Serine-43) of  the Thermoplasma acidophilum citrate synthase. Serine-309 Cysteine mutation drastically reduced the  activity, as well as the thermostabiity of the enzyme. Although Serine-43 Cysteine mutation reduced  the enzyme activity, it did not have any effect on the thermostability. Both wild-type and cysteine-43  mutant Thermoplasma citrate synthase enzymes were purified to homogenity using affinity  chromatography on Matrex Gel Red A. The cysteine-43 mutant Thermoplasma citrate synthase was  strikingy similar to the wild-type recombinant citrate synthase in its molecular size, substrate and co-factor  specificities, pH profile and thermal resistance. The decrease in the specific activity of the citrate  synthase as a result of this mutation was reflected by V max and E a values.

 

Two cysteine residues were introduced to selected positions (Serine-309 and Serine-43) of  the Thermoplasma acidophilum citrate synthase. Serine-309 Cysteine mutation drastically reduced the  activity, as well as the thermostabiity of the enzyme. Although Serine-43 Cysteine mutation reduced  the enzyme activity, it did not have any effect on the thermostability. Both wild-type and cysteine-43  mutant Thermoplasma citrate synthase enzymes were purified to homogenity using affinity  chromatography on Matrex Gel Red A. The cysteine-43 mutant Thermoplasma citrate synthase was  strikingy similar to the wild-type recombinant citrate synthase in its molecular size, substrate and co-factor  specificities, pH profile and thermal resistance. The decrease in the specific activity of the citrate  synthase as a result of this mutation was reflected by V max and E a values.

Makale detayları

Purification and Characterization of Cysteine-43 Mutant Citrate Synthase from Thermoplasma acidophilum

Yazarlar:

İpek ERDURAN

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 1999 Vol.23 Issue 4, pp.423-432

Belge Tipi:

Makale

Yayın Tarihi:

3/1999

Belge Dili:

Türkçe

Document ID (Org No.):

2000814193

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152

Thermostability

Thermoplasma acidophium

citrate synthase

site-specific mutagenesis.

Sayı

Makale detayları

Purification and Characterization of Cysteine-43 Mutant Citrate Synthase from Thermoplasma acidophilum

Yazarlar: İpek ERDURAN

Yayıncı: TUBITAK

Dergi: Turkish Journal of Biology 1999 Vol.23 Issue 4, pp.423-432

Belge Tipi: Makale

Yayın Tarihi: 3/1999

Belge Dili: Türkçe

Document ID (Org No.): 2000814193

Sıklık: İki Aylık

eISSN: 1303-6092

pISSN: 1300-0152

Thermostability

Thermoplasma acidophium

citrate synthase

site-specific mutagenesis.

Sayı

Yazarlar:

İpek ERDURAN

Yayıncı:

TUBITAK

Dergi:

Turkish Journal of Biology 1999 Vol.23 Issue 4, pp.423-432

Belge Tipi:

Makale

Yayın Tarihi:

3/1999

Belge Dili:

Türkçe

Document ID (Org No.):

2000814193

Sıklık:

İki Aylık

eISSN:

1303-6092

pISSN:

1300-0152