Martínez J, Henriksson J, Ridåker M, Pettersson U, Cazzulo J J
Instituto de Investigaciones Bioquímicas Luis F. Leloir, CONICET, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires, Argentina.
FEMS Microbiol Lett. 1998 Feb 1;159(1):35-9. doi: 10.1111/j.1574-6968.1998.tb12838.x.
Forty-eight cDNA clones obtained from different developmental stages of Trypanosoma cruzi and all encoding the C-terminal domain of the major cysteine proteinase (cruzipain) have been sequenced. A number of polymorphisms were detected, seven of them resulting in amino acid replacements. The predicted pI values of the corresponding gene products varied between 7.05 and 8.12. These changes in amino acid sequence, together with previously reported variations in carbohydrate composition at the only N-glycosylation site in the C-terminal domain, may account for most of the heterogeneities found in the mature enzyme.
从克氏锥虫不同发育阶段获得的48个cDNA克隆已被测序，这些克隆均编码主要半胱氨酸蛋白酶（克氏锥虫蛋白酶）的C末端结构域。检测到了许多多态性，其中7个导致氨基酸替换。相应基因产物的预测pI值在7.05至8.12之间变化。氨基酸序列的这些变化，连同先前报道的C末端结构域中唯一N-糖基化位点处碳水化合物组成的变化，可能是成熟酶中发现的大多数异质性的原因。
