Titani K, Torff H J, Hormel S, Kumar S, Walsh K A, Rödl J, Neurath H, Zwilling R
Biochemistry. 1987 Jan 13;26(1):222-6. doi: 10.1021/bi00375a029.
The amino acid sequence of a protease from the crayfish Astacus fluviatilis has been determined from overlapping sets of peptides derived largely by cleavage at Met, Lys, or Arg residues. The protein comprises 200 amino acid residues in a single polypeptide chain, corresponding to a molecular mass of 22,614 daltons. Two disulfide bonds link Cys-42 to Cys-198 and Cys-64 to Cys-84. The sequence of this invertebrate protease appears to be unique since it has no homologous relationship to any of the known protein sequences.
对源自淡水小龙虾(Astacus fluviatilis)的一种蛋白酶的氨基酸序列进行了测定,该序列主要来自于通过在甲硫氨酸、赖氨酸或精氨酸残基处切割而获得的重叠肽段集合。该蛋白质由一条单多肽链中的200个氨基酸残基组成,对应分子量为22,614道尔顿。两条二硫键将半胱氨酸-42与半胱氨酸-198相连,半胱氨酸-64与半胱氨酸-84相连。这种无脊椎动物蛋白酶的序列似乎是独特的,因为它与任何已知蛋白质序列均无同源关系。