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研究了在Ｃａ２＋ 存在下荞麦花粉肽及其类似物和丹磺酰标记的钙调素（Ｄ－ＣａＭ）的相互作用， 结果表明， 除肽ＢＰ－１ 外， 都能与Ｄ－ＣａＭ 结合而形成复合物． 利用荧光光谱法测定了这些复合物的解离常数Ｋｄ． 在所研究的多肽中以ＢＰ－１３ 拮抗ＣａＭ 作用最强， 其Ｋｄ 值为４．６×１０－ ２μｍ ｏｌ／Ｌ， 抑制钙依赖性磷酸二酯酶活性的ＩＣ５０为２．２ μｍ ｏｌ／Ｌ． 我们还发现， 当Ｄ－丙氨酸残基取代没有亲和性的ＢＰ－１ 中甘氨酸残基时， 其亲和性明显提高．
The interaction of buckwheat pollen peptides and their analogues with dansyl-labeled calmodulin (D-CaM) in the presence of Ca2 + was studied and the results show that all but the peptide BP-1 can be combined with D-CaM to form Complex. The dissociation constants Kd of these complexes were measured by fluorescence spectroscopy. Among the studied peptides, BP-13 had the strongest antagonistic effect on CaM with a Kd value of 4.6 × 10-2 μmol / L and an IC50 of inhibiting calcium-dependent phosphodiesterase activity of 2.2 μmol / L . We also found that D-alanine residues have significantly improved affinity when they substitute for glycine residues in BP-1 without affinity.