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M F Tecce

Publications and source records attributed to M F Tecce.

23 records · Page 2Linked to original sources
PubMed1983

A four- to sixfold enhancement in sensitivity for detecting trace proteins in dye or silver stained polyacrylamide gels.

A very simple procedure which enhances sensitivity in visualizing proteins stained by all standard procedures in polyacrylamide gels is described. The process, based on the use of concentrated polyethylene glycol 6000 solutions, produces a conspicuous, reversible, and uniform size reduction of gels. The entity of the reduction depends principally on the polyethylene glycol 6000 concentration and on the acrylamide content of gels. Using an appropriate polyethylene glycol 6000 concentration, it is possible to regulate the final size and then the sensitivity as needed. Depending upon the above conditions it is possible to increase the sensitivity by a factor of 4-6 or more. Reduction of the gel volume by such a factor may eliminate the need for the cumbersome and frequently impossible preconcentration of samples. Besides the Coomassie blue stained gels, silver stained gels may also be treated in a similar manner with a consequent further enhancement in sensitivity. In addition, gels containing radiolabeled materials can be autoradiographed in times proportionally shorter, without significant sacrifice of resolution.

Coloring Agents↗
PubMed1983

Evidence for homologous repeating segments within the elementary polypeptide chain of guinea pig thyroglobulin.

In this paper we report on the peptide maps of the three polypeptides produced by reduction of denatured 19-S thyroglobulin from guinea pig. These maps were obtained by both chemical cleavage (CNBr) and by limited enzymatic proteolysis (Staphylococcus aureus SV 8 protease). Analysis of these peptides showed a strict correspondence among the electrophoretic bands produced by cleavage of the guinea pig thyroglobulin components. These results support the idea that thyroglobulin, even though it has an apparently complex molecular structure, contains polypeptide sequences which are repeated in the elementary chain. Since similar structures should correspond to similar functions, each of these regions may work as a functional domain for the biosynthesis of the thyroid hormones.

Animals↗
PubMedDate not supplied

Monoclonal antibodies recognizing a recombinant portion of human alpha-fetoprotein with antigenic selectivity versus albumin.

Determination of serum alpha-fetoprotein is useful in the clinical management of liver cancer, but it has not been particularly helpful in the early diagnosis of this disease, since also non-neoplastic liver diseases may result in small increases of its serum concentration. To improve the clinical performance of this assay, we have previously developed an in vitro culture system, in which the expression of alpha-fetoprotein and albumin could be coordinately modulated by thyroid hormone. This system allowed large scale production and purification of native alpha-fetoprotein to be used as reference material. In addition, we synthesized and cloned in a bacterial expression vector a DNA sequence coding of human alpha-fetoprotein amino acid sequence 38-119. This alpha-fetoprotein sequence was chosen since it is the least homologous to albumin, being the amino acid sequence of the two proteins extremely similar with an overall identity of about 38%. Now we have obtained three hybridomas recognizing with high affinity and specificity both the recombinant fragment and native alpha-fetoprotein. These antibodies, which therefore recognize the native protein in the amino acid sequence 38-119, should allow the development of an immunoassay for alpha-fetoprotein with absolute selectivity versus albumin. This might result in more sensitive clinical determinations, avoiding the possibility of cross-reactions.

Albumins↗