Benishin C G, Lewanczuk R Z, Shan J, Pang P K
Department of Physiology, University of Alberta, Edmonton, Canada.
J Cardiovasc Pharmacol. 1994;23 Suppl 2:S9-13.
Parathyroid hypertensive factor (PHF) has been purified from two sources of material: plasma of spontaneously hypertensive rats (SHRs) and culture medium from organ culture of SHR parathyroid glands. Chromatographic characteristics of PHF from these two sources are identical. Biological activity of PHF (assayed as the characteristic delayed hypertensive response in normotensive rats) is sensitive to degradation by treatment in base, and the enzymes trypsin, chymotrypsin, phospholipase C, and phospholipase D. PHF activity may also be extracted from source material with chloroform: methanol (4:1). A hypothetical structure for the active component of PHF is suggested. This is comprised of a peptide liked to a lysophospholipid.
甲状旁腺高血压因子（PHF）已从两种来源的材料中纯化出来：自发性高血压大鼠（SHR）的血浆和SHR甲状旁腺器官培养的培养基。来自这两种来源的PHF的色谱特征是相同的。PHF的生物活性（以正常血压大鼠中特征性的延迟性高血压反应来测定）对碱处理、以及胰蛋白酶、糜蛋白酶、磷脂酶C和磷脂酶D的酶解敏感。PHF活性也可用氯仿：甲醇（4:1）从原料中提取。提出了PHF活性成分的一种假设结构。它由与溶血磷脂相连的肽组成。
