Application of tandem fast protein liquid chromatography to purify intact native monomeric/aggregated Tamm-Horsfall protein from the human urine and systematic comparisons with diatomaceous earth adsorption and salt precipitation: Yield, purity and time-consumption

2021 ◽  
Author(s):  
Chadanat Noonin ◽  
Chompunoot Kapincharanon ◽  
Kanyarat Sueksakit ◽  
Rattiyaporn Kanlaya ◽  
Visith Thongboonkerd

Tamm-Horsfall protein (THP) is a high-abundance urinary protein. Although its functions have been studied for years, several aspects of those remain unclear. To achieve more knowledge on THP functions, effective...

1991 ◽  
Vol 46 (9-10) ◽  
pp. 850-855 ◽  
Author(s):  
John V. Dean ◽  
John W. Gronwald ◽  
Michael P. Anderson

Abstract Fast protein liquid chromatography (anion exchange) was used to separate glutathione S-transferase isozymes in nontreated etiolated maize shoots and those treated with the herbi­cide safener CGA -1542814-(dichloroacetyl)-3,4-dihydro-3-methyl-2 H-1 ,4-benzoxazine. Non­treated shoots contained isozymes active with the following substrates: trans-cinnamic acid (1 isozyme), atrazine (3 isozymes), 1-chloro-2,4-dinitrobenzene (1 isozyme), metolachlor (2 isozymes) and the sulfoxide derivative of S-ethyl dipropylcarbamothioate (2 isozymes). Pre­treatment of shoots with the safener CGA -154281 (1 μM) had no effect on the activity of the isozymes selective for trans-cinnamic acid and atrazine but increased the activity of the constitutively-expressed isozymes that exhibit activity with 1-chloro-2,4-dinitrobenzene, metola­chlor and the sulfoxide derivative of S-ethyl dipropylcarbamothioate. The safener pretreat­ment also caused the appearance of one new isozyme active with 1-chloro-2,4-dinitrobenzene and one new isozyme active with metolachlor. The results illustrate the complexity of gluta­thione S-transferase activity in etiolated maize shoots, and the selective enhancement of gluta­thione S-transferase isozymes by the safener CGA -154281.


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