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F Franĕk

Publications and source records attributed to F Franĕk.

At least 55 records · Page 3Linked to original sources
PubMed1977

Amino acid sequence of normal (microheterogeneous) porcine immunoglobulin lambda chains.

The partial amino acid sequence of pooled, microheterogeneous pig immunoglobulin lambda chains was determined previously (Franĕk, F. (1970), FEBS Lett. 8, 269; Novotný, J., and Franĕk, F. (1975), FEBS Lett. 58, 24). In the present study, citraconylated pig lambda chains were digested by trypsin under conditions in which some of the epsilon-amino groups of lysine residues unmask. The resulting fragments were purified by gel filtration and ion-exchange chromatography at pH 3.0 in buffers containing urea; some of the fragments were found to be of intermediate size (i.e., larger than normal tryptic peptides but smaller than "citraconyl" peptides), thus permitting overlap information and amino acid sequences of all the 14 tryptic peptides to be deduced from amino acid compositions and partial amino acid sequences of selected fragments. In addition to completing the major amino acid sequence of pig immunoglobulin lambda chains, the present study demonstrates that it is possible to sequence microheterogeneous proteins with a suitable fragmentation strategy.

Amino Acid Sequence↗
PubMed1976

The amino-terminal sequence of the VHIII subgroup of pooled porcine IgG.

Pig gamma-chains contain a significant fraction of the unblocked VHIII variable region subgroup. The amino terminal sequence (30 residues) was found to be uniform and more than 90% homologous with the prototype sequence of the human VHIII subgroup. An additional VHIII phylogenetically associated residue, glutamic acid in position 2 was identified in these porcine heavy chains.

Amino Acid Sequence↗
PubMed1975

Inactivation of hapten-modified bacteriophage by antibody: increased sensitivity of the assay in media containing polyethylene glycol.

Inactivation of dinitrophenylated bacteriophage T4 by porcine and rabbit anti-dinitrophenyl (DNP) antibodies was studied by the complex inactivation methods. The inactivation titers increased 20-30 times when polyethylene glycol, mol. wt. 6000, was added to the incubation media. Consequently, the detection of dinitrophenylated serum albumin with the modified bacteriophage could be carried out with higher sensitivity upon addition of polyethylene glycol.

Antibodies↗