外源DNA在体内的吸收与降解

外源ＤＮＡ在动物体内的吸收与降解研究已经受到了关注[1、2 ] 。由于基因治疗与ＤＮＡ疫苗的飞速发展 ,经常要通过一定的方式将外源的ＤＮＡ导入到动物体 ,然而对于它们的吸收与降解机制到目前为止仍然不是十分清楚。用基因治疗疾病时 ,须解决外源基因在动物体内的吸收与降解问题 ,尤其是大量外源ＤＮＡ质粒在动物体内的吸收与降解问题。外源ＤＮＡ的吸收与降解研究已成为一个热点 ,目前主要集中在肠胃道吸收降解和细胞吸收降解两个方面。1 .外源ＤＮＡ在肠胃道中的吸收与降解最有可能让外源ＤＮＡ进入动物体的就是肠胃道 ,在每天的进食中 …     

多效唑（MET）对啤酒花试管苗生长和移栽的影响

在培养基中加入0.1-0.2mg/L浓度的多效唑（MET）,啤酒花试管苗植株矮壮,单株生根数量增加、移栽成活率提高13％。0．5－2．0mg/L时,试管苗基部愈伤组织增多,枝叶失绿,生长受到抑制。初步发现多将唑对啤酒花试管苗的效力与葡萄糖用量呈正相关。     

Macromolecular substrate affinity for the tissue factor-factor VIIa complex is independent of scissile bond docking.

The upstream coagulation enzymes are homologous trypsin-like serine proteases that typically function in enzyme-cofactor complexes, exemplified by coagulation factor VIIa (VIIa), which is allosterically activated upon binding to its cell surface receptor tissue factor (TF). TF cooperates with VIIa to create a bimolecular recognition surface that serves as an exosite for factor X binding. This study analyzes to what extent scissile bond docking to the catalytic cleft contributes to macromolecular substrate affinity. Mutation of the P1 Arg residue in factor X to Gln prevented activation by the TF.VIIa complex but did not reduce macromolecular substrate affinity for TF.VIIa. Similarly, mutations of the S and S' subsites in the catalytic cleft of the enzyme VIIa failed to reduce affinity for factor X, although the affinity for small chromogenic substrates and the efficiency of factor X scissile bond cleavage were reduced. Thus, docking of the activation peptide bond to the catalytic cleft of this enzyme-cofactor complex does not significantly contribute to affinity for macromolecular substrate. Rather, it appears that the creation of an extended macromolecular substrate recognition surface involving enzyme and cofactor is utilized to generate substrate specificity between the highly homologous, regulatory proteases of the coagulation cascade.