DeFeudis F V, Orensanz Muñoz L M, Vidal M A, Corrochano G, Sanchez del Alamo M
Experientia. 1978 Sep 15;34(9):1169-70. doi: 10.1007/BF01922937.
High-affinity, Na+-independent binding of beta-alanine to a synaptosomal fraction of rat brain was potently inhibited by glycine and by some other alpha-amino acids, but not by taurine or GABA. This binding mechanism, which was also sensitive to both bicuculline and strychnine, might involve synaptic receptors for both beta-alanine and glycine.
β-丙氨酸与大鼠脑突触体部分的高亲和力、不依赖钠离子的结合受到甘氨酸和其他一些α-氨基酸的强烈抑制,但不受牛磺酸或γ-氨基丁酸的抑制。这种结合机制对荷包牡丹碱和士的宁均敏感,可能涉及β-丙氨酸和甘氨酸的突触受体。