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鏈霉親和素分子由4條相同的肽鏈組成，其氨基酸組成中，甘氨酸和丙氨酸的含量較大，而且結(jié)合生物素的活性基團也是肽鏈中的色氨酸殘基；

鏈霉親和素是一種稍偏酸性（pH6.0）的蛋白質(zhì)，并且不帶任何糖基。

在蛋白水解酶作用下，鏈霉親和素可在N端10～12和C端19-21間斷裂，形成的核心鏈霉親和素仍然保持完整的結(jié)合生物素的能力，所以可以提高融合率。

鏈霉親和素是與親和素有相似生物學(xué)特性的一種蛋白質(zhì)，是鏈霉菌的分泌物，其分子量及結(jié)合生物素的能力與雞蛋清中的親和素相似，等電點6.0，非特異性結(jié)合遠比親和素低。

Streptavidin molecule is composed of four identical peptide chains. In its amino acid composition, the contents of glycine and alanine are large, and the active group binding biotin is also tryptophan residue in the peptide chain;

Streptavidin is a slightly acidic (pH 6.0) protein without any sugar groups.

Under the action of proteolytic enzyme, streptavidin can break between N-terminal 10-12 and C-terminal 19-21, and the formed core streptavidin still maintains the complete ability to bind biotin, so the fusion rate can be improved.

Streptavidin is a protein with similar biological characteristics to avidin. It is the secretion of Streptomyces. Its molecular weight and ability to bind biotin are similar to avidin in egg white. Its isoelectric point is 6.0, and its nonspecific binding is much lower than avidin.