Partial purification and characterization of arylamine N-acetyltransferases from human breast tumor tissues

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2006

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Su, Yaşasın Senem

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Arylamine N-acetyltransferases (NATs) were partially purified from human breast tumor tissues with complete separation of the isoforms in DEAE-Cellulose ion-exchange step. NAT with activity towards p-aminobenzoic acid (PABA) was isolated and purified from human breast tumor with 77 % yield and a purification factor of 5-fold. NAT with activity towards sulfamethazine (SMZ) was isolated and purified from human breast tumor with 21 % yield and a purification factor of 3-fold. Further purification attempts by Blue Sepharose affinity column chromatography resulted in the complete loss of both enzyme activities. The NAT1 purified from human breast tumor tissues had a molecular weight (Mr) value of about 27600 and an isoelectric point (pI) around 4.8, as confirmed by SDS-PAGE, IEF and Western blotting analysis. With immunohistochemical analysis, level of intensity of NAT1 immunostaining was observed to be going from weak in reduction mammoplasty samples to strongest in malignant breast tissue. The interindividual variation in the conjugation of p-aminobenzoic acid (PABA) and of sulfamethazine (SMZ) by cytosolic arylamine N-acetyltransferases (NATs) were investigated in 30 human breast tumor and matched samples. The average specific activity against PABA was calculated as 13?2 pmole/min/mg protein for breast control NATs, and 20?3 pmole/min/mg protein for breast tumor NATs. The average specific activity against SMZ was calculated as 12?2 pmole/min/mg protein for breast control NATs, and 34?6 pmole/min/mg protein for breast tumor NATs. Wilcoxon test revealed that the difference between the control and tumor groups is statistically significant with respect to the NAT1 activities as well as NAT2 activities.

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Biology.

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http://etd.lib.metu.edu.tr/upload/3/12607023/index.pdf
https://hdl.handle.net/11511/15740

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Graduate School of Natural and Applied Sciences, Thesis

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Citation Formats

Y. S. Su, “Partial purification and characterization of arylamine N-acetyltransferases from human breast tumor tissues,” Ph.D. - Doctoral Program, Middle East Technical University, 2006.