Abstract: Two acylphosphatase molecular forms have been isolated from bovine testis. Their amino acid sequence was determined. One (ACY1) consists of 98 amino acid residues, while the other one (ACY2) consists of 100 amino acid residues. Both molecular forms are N-acetylated and differ only in the amino terminus. ACY2 has an additional Ser-Met tail with respect to ACY1. Both ACY1 and ACY2 are organ-common type isoenzymes and thus differ for about half of the amino acid positions from the previously sequenced bovine muscle isoenzyme.
Bovine testis acylphosphatase: purification and amino acid sequence / L. Pazzagli; G. Cappugi; G. Camici; G. Manao; G. Ramponi. - In: JOURNAL OF PROTEIN CHEMISTRY. - ISSN 0277-8033. - STAMPA. - 12:(1993), pp. 593-601.
Bovine testis acylphosphatase: purification and amino acid sequence
PAZZAGLI, LUIGIA;CAPPUGI, GIANNI;CAMICI, GUIDO;MANAO, GIAMPAOLO;RAMPONI, GIAMPIETRO
1993
Abstract
Abstract: Two acylphosphatase molecular forms have been isolated from bovine testis. Their amino acid sequence was determined. One (ACY1) consists of 98 amino acid residues, while the other one (ACY2) consists of 100 amino acid residues. Both molecular forms are N-acetylated and differ only in the amino terminus. ACY2 has an additional Ser-Met tail with respect to ACY1. Both ACY1 and ACY2 are organ-common type isoenzymes and thus differ for about half of the amino acid positions from the previously sequenced bovine muscle isoenzyme.
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