Homogeneous bovine prolactin (bPRL) has been obtained using a procedure based on high-performance anion-exchange chromatography. The procedure enables up to 6 mg of 99.4% pure bPRL to be obtained per hour, with a recovery of 32.4%. The purity of the protein was checked by N-terminal sequencing and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The highly purified bPRL obtained with this method is suitable for complete structural and immunochemical studies.

Purification to homogeneity of bovine prolactin by high-performance ion-exchange chromatography / A. Berrini, V. Borromeo, C. Secchi. - In: JOURNAL OF CHROMATOGRAPHY A. - ISSN 1873-3778. - 547:1-2(1991), pp. 457-461.

Purification to homogeneity of bovine prolactin by high-performance ion-exchange chromatography

A. Berrini
;
V. Borromeo
Secondo
;
C. Secchi
Ultimo
1991

Abstract

Homogeneous bovine prolactin (bPRL) has been obtained using a procedure based on high-performance anion-exchange chromatography. The procedure enables up to 6 mg of 99.4% pure bPRL to be obtained per hour, with a recovery of 32.4%. The purity of the protein was checked by N-terminal sequencing and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The highly purified bPRL obtained with this method is suitable for complete structural and immunochemical studies.
Growth-hormone; electrophoresis; variants; forms
Settore BIO/12 - Biochimica Clinica e Biologia Molecolare Clinica
Settore VET/02 - Fisiologia Veterinaria
1991
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/513156
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