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Biomedical subjects

J Liberatori

Publications and source records attributed to J Liberatori.

6 recordsLinked to original sources
PubMed1979

beta-lactoglobulins in the mammary secretions of camel (Camelus dromedarius) and she-ass. Immunological detection and preliminary physico-chemical characterization.

The mammary secretions of a monogastric, the ass, and those of a Tylopode, the camel (camelus dromedarius), were examined by double diffusion in agarose gel against rabbit sera anti-bovine beta-lactoglobulin. Clear precipitin reactions were obtained. After immunoelectrophoresis the camel and she-ass beta-lactoglobulins showed very different electrophoretic mobilities.

Animals↗
PubMed1979

Immunochemical studies on beta-lactoglobulins. precipitin reactions of sow's and mare's mammary secretions against anti - bovine beta - lactoglobulin antiserum.

By double diffusion in agarose gel, in well defined experimental conditions, cross reactions were observed between porcine beta-lactoglobulins and anti-bovine beta-lactoglobulin antisera. The immunological reactivity between these beta-lactoglobulins from a monogastric and the ruminant anti beta-lactoglobulin antiserum thus implies a certain degree of similarity between the monomeric beta-lactoglobulins examined and the dimeric of the ruminants. With the same antisera it also proved possible to demonstrate the presence of beta-lactoglobulins in the mammary secretions of another monogastric, namely, the mare. Identity reactions observed between sow's and mare's beta-lactoglobulins seem to indicate a close similarity in their structures.

Animals↗
PubMed1979

Immunological evidence of beta-lactoglobulins in human colostrum and milk.

Over thirty specimens of breast milk and colostrum were examined by the double diffusion method in agarose gel using antibovine beta-lactoglobulin antisera. Cross reactions were obtained showing the presence of beta-lactoglobulins in human milk and colostrum; the strength of these reactions was comparable with those already observed with porcine and equine mammary secretions. Identity reactions were obtained between human and sow's milk against anti-bovine beta-lactoglobulin antisera. Results are discussed from the immunological and structural point of view.

Animals↗
PubMedDate not supplied

The primary structure of the beta-lactoglobulin of the waterbuffalo (Bubalus arnee).

The complete amino acid sequence of the beta-lactoglobuline of the waterbuffalo (Bubalus arnee) was established. The sequence of peptides obtained by cleavage with BNPS-Skatole, CNBr and trypsin were determined automatically by the help of the sequenator. Only two differences were found in the beta lactoglobulin of the waterbuffalo compared with the bovine beta-lactoglobulin B.

Amino Acid Sequence↗