A comparison of both amino acid composition and sequence of the rabbit uteroglobin (UG) subunit and the rat seminal vesicle sperm-binding protein (rSBP) by computer analysis indicates homology between the two polypeptide chains. These findings are supported by immunological studies showing the occurrence of similar antigenic determinants. In addition, our data indicate the glutamine-9 of the rat seminal vesicle sperm-binding protein and glutamine-40 of UG as the possible glutamine residues involved when the proteins act as transglutaminase (TGase) substrates. The latter results represent an interesting approach to determining the general structural features of the acyl donor site in the TGase-catalyzed reaction.
Homology Between Rabbit Uteroglobin and the Rat Seminal-vesicle Sperm-binding Protein - Prediction of Structural Features of Glutamine Substrates For Transglutaminase / S., Metafora; F., Facchiano; A., Facchiano; C., Esposito; G., Peluso; Porta, Raffaele. - In: JOURNAL OF PROTEIN CHEMISTRY. - ISSN 0277-8033. - STAMPA. - 6:(1987), pp. 353-359. [10.1007/BF00248054]
Homology Between Rabbit Uteroglobin and the Rat Seminal-vesicle Sperm-binding Protein - Prediction of Structural Features of Glutamine Substrates For Transglutaminase
PORTA, RAFFAELE
1987
Abstract
A comparison of both amino acid composition and sequence of the rabbit uteroglobin (UG) subunit and the rat seminal vesicle sperm-binding protein (rSBP) by computer analysis indicates homology between the two polypeptide chains. These findings are supported by immunological studies showing the occurrence of similar antigenic determinants. In addition, our data indicate the glutamine-9 of the rat seminal vesicle sperm-binding protein and glutamine-40 of UG as the possible glutamine residues involved when the proteins act as transglutaminase (TGase) substrates. The latter results represent an interesting approach to determining the general structural features of the acyl donor site in the TGase-catalyzed reaction.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
