Cohen-Solal L, Castanet J, Meunier F J, Glimcher M J
Comp Biochem Physiol B. 1986;83(2):483-6. doi: 10.1016/0305-0491(86)90399-8.
Extent of prolyl hydroxylation in newly synthesized viper collagen is decreased at 10 degrees C to approximately 23% of normal on skin and to approximately 57% of normal in bone collagen. At 20 degrees C, prolyl hydroxylation is approximately 50% of normal in skin and normal in bone. At 10 degrees C and 20 degrees C, prolyl hydroxylation is decreased approximately 32% in the skin collagen of carp. In contrast, prolyl hydroxylation is unchanged at 10 and 20 degrees C in bone, scale and lepidotrichia. Prolyl hydroxylation of cartilaginous endoskeleton showed an approximately 25% decrease at 20 degrees C.
在10摄氏度时,新合成的蝰蛇胶原蛋白中脯氨酰羟化程度降低,皮肤中降至正常水平的约23%,骨胶原蛋白中降至正常水平的约57%。在20摄氏度时,皮肤中脯氨酰羟化约为正常水平的50%,骨中为正常水平。在10摄氏度和20摄氏度时,鲤鱼皮肤胶原蛋白中的脯氨酰羟化降低约32%。相比之下,在10摄氏度和20摄氏度时,骨、鳞片和鳍条中的脯氨酰羟化没有变化。软骨内骨骼的脯氨酰羟化在20摄氏度时显示约25%的降低。