Purification of testicular anti-Müllerian hormone allowing direct visualization of the pure glycoprotein and determination of yield and purification factor
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2016, Veterinary Clinics of North America - Equine PracticeCitation Excerpt :Subsequent experiments demonstrated that AMH was a glycoprotein,5,6 which contained disulfide bridges as smaller fragments were obtained when preparations of fetal testes were examined using sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions.6 As the methods of AMH purification improved, more detailed information was obtained about the physical properties of this glycoprotein7 as well as its biochemical composition with respect to amino acids and carbohydrates.8,9 The protein AMH is derived from a precursor that varies slightly in length among different species, ranging from 553 (rat) to 575 (bovine) amino acids.3
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