Barthélémy M, Péduzzi J, Ben Yaghlane H, Labia R
Muséum National Histoire Naturelle, CNRS UA 401, Paris, France.
FEBS Lett. 1988 Apr 11;231(1):217-20. doi: 10.1016/0014-5793(88)80734-8.
SHV-2 beta-lactamase was purified from an overproducing variant of a clinical isolate of Escherichia coli resistant to cefotaxime. Pure protein was digested by trypsin and Lys-C endoproteinase. Proteolytic peptides, isolated by reverse-phase HPLC, were submitted to manual Edman degradation and aligned by homology with the sequence of SHV-1 beta-lactamase. A putative amino acid sequence was deduced. Structural comparison revealed that SHV-2 differed from SHV-1 by only one amino acid, Gly----Ser, at position 213 of the mature protein.
超广谱β-内酰胺酶2（SHV-2）是从一株对头孢噻肟耐药的大肠埃希菌临床分离株的高产变异株中纯化得到的。纯蛋白用胰蛋白酶和Lys-C内切蛋白酶进行消化。通过反相高效液相色谱分离得到的蛋白水解肽段，进行手动埃德曼降解，并与超广谱β-内酰胺酶1（SHV-1）的序列进行同源比对。推导得到一个假定的氨基酸序列。结构比较显示，成熟蛋白第213位氨基酸处，SHV-2与SHV-1仅存在一个氨基酸差异，即甘氨酸（Gly）变为丝氨酸（Ser）。
