form
saline suspension
extent of labeling
≥6 mg per mL
matrix
crosslinked 4% beaded agarose
matrix activation
cyanogen bromide
matrix attachment
amino
matrix spacer
1 atom
storage temp.
2-8°C
Application
p-Aminomethylbenzenesulfonamide is an agarose in saline suspension that can be used in affinity chromatography, protein chromatography and specialty resins. p-Aminomethylbenzenesulfonamide has been used in studies assessing inhibition of mitochondrial carbonic anhydrase and ureagenesis.
Physical form
Suspension in 0.5 M NaCl containing preservative.
D K Srivastava et al.
Journal of the American Chemical Society, 129(17), 5528-5537 (2007-04-05)
Despite the similarity in the active site pockets of carbonic anhydrase (CA) isozymes I and II, the binding affinities of benzenesulfonamide inhibitors are invariably higher with CA II as compared to CA I. To explore the structural basis of this
B Ulmasov et al.
Proceedings of the National Academy of Sciences of the United States of America, 97(26), 14212-14217 (2000-12-20)
Carbonic anhydrase XII (CA XII) is a transmembrane glycoprotein with an active extracellular CA domain that is overexpressed on cell surfaces of certain cancers. Its expression has been linked to tumor invasiveness. To characterize its catalytic properties, we purified recombinant
S J Dodgson et al.
Journal of applied physiology (Bethesda, Md. : 1985), 60(2), 646-652 (1986-02-01)
The amount of urea produced in 60 min, [urea]t = 60, from intact guinea pig hepatocytes incubated in NH4Cl, oleate, lactate, NaHCO3, and ornithine at 37 degrees C at pH 7.1 is decreased by ethoxzolamide (EZ): Ki,EZ [urea]t = 60
S J Dodgson et al.
Archives of biochemistry and biophysics, 251(1), 198-204 (1986-11-15)
The carbonic anhydrase inhibitor acetazolamide reduces citrulline synthesis by intact guinea pig liver mitochondria and also inhibits mitochondrial carbonic anhydrase (CA V) and the more lipophilic carbonic anhydrase inhibitor ethoxzolamide reduces urea synthesis by intact guinea pig hepatocytes in parallel
P R Conliffe et al.
Molecular and cellular endocrinology, 106(1-2), 121-130 (1994-12-01)
Prolactin-like protein C (PLP-C) is a member of the rat placental family of proteins which are structurally related to pituitary prolactin (PRL). In an effort to characterize the receptor specificity and biological activity of PLP-C, we used a PLP cDNA
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