Biomedical subjects

A Krust

Publications and source records attributed to A Krust.

43 records · Page 3Linked to original sources

PubMed1979

Cloning of an almost full-length chicken conalbumin double-stranded cDNA.

Chicken conalbumin double-stranded cDNA (con-dscDNA) was synthesized from a laying hen oviduct mRNA preparation enriched for conalbumin mRNA (con-mRNA). The dscDNA was inserted by blunt-end ligation into the Sal I site of plasmid pBR322 which had been repaired with DNA polymerase I to create Taq I sites on each side of the inserted fragment. After bacterial transformation, one hybrid recombinant, pBR322-con1, which contains the largest inserted dscDNA (about 2350 bp) was shown to hybridize specifically to the RNA which is translated into conalbumin. Electron microscopic examination of hybrid molecules between con-mRNA and pBR322-con1 DNA indicate that the inserted con-dscDNA is an almost full-length double-stranded transcript of conalbumin mRNA.

Animals↗

PubMed1978

Synthesis of an ovalbumin-like protein by Escherichia coli K12 harbouring a recombinant plasmid.

A cloned DNA transcript of ovalbumin mRNA was cut a few nucleotides away from the initiator codon, and fused in phase to the beginning of the Escherichia coli beta-galactosidase gene. The hybrid gene has been cloned in E. coli where it produces large amounts of an ovalbumin-like protein.

Codon↗

PubMed1978

Isolation by molecular cloning of a fragment in the split ovalbumin gene.

An EcoRI fragment of chicken DNA (fragment 'a') containing a sequence complementary to the 3' half of ovalbumin mRNA has been isolated by molecular cloning. Analysis of the cloned fragment proves conclusively that the chicken ovalbumin gene is split. Fragment 'a' contains no extensive sequence repeated elsewhere in the genome and represents the only type of organisation of this part of the split ovalbumin gene in chicken genome.

Animals↗

PubMed1978

The ovalbumin split gene: molecular cloning of Eco RI fragments "c" and "d".

The Eco RI fragments "c" and "d" of the ovalbumin gene (1, 2) have been isolated by molecular cloning. Restriction enzyme mapping and electron microscopy have confirmed that the two fragments contain the same ovalbumin mRNA coding sequences. These sequences are split into two regions which have been mapped in fragments "c" and "d". There is no evidence that the ovalbumin mRNA sequences contained in these fragments could be further interrupted. Our results confirm that the presence of Eco RI fragment "d" in some chickens is due to the existence of an allelic variant of the ovalbumin gene which contains an additional Eco RI site within the region corresponding to Eco RI fragment "c". This additional Eco RI site appears to be the main difference between the two alleles. Finally, our results provide a direct demonstration that most of the ovalbumin mRNA sequences are encoded for by Eco RI fragments "a", "b" and "c".

Coliphages↗

PubMed1977

Molecular cloning of extensive sequences of the in vitro synthesized chicken ovalbumin structural gene.

Double-stranded DNA molecules complementary to ovalbumin chicken messenger RNA were synthesized in vitro and integrated into the E. coli plasmid pCR1 using an oligodG-dc tailing procedure. The resultant hybrid plasmids, amplified by transfection of E. coli, were shown by hybridization and gel electrophoresis to contain extensive DNA sequences of the ovalbumin structural gene.

Animals↗

PubMedDate not supplied

Human oestrogen receptor cDNA: sequence, expression and homology to v-erb-A.

We have cloned and sequenced the complete complementary DNA of the oestrogen receptor (ER) present in the breast cancer cell line MCF-7. The expression of the ER cDNA in HeLa cells produces a protein that has the same relative molecular mass and binds oestradiol with the same affinity as the MCF-7 ER. There is extensive homology between the ER and the erb-A protein of the oncogenic avian erythroblastosis virus.

Amino Acid Sequence↗

PubMedDate not supplied

A human retinoic acid receptor which belongs to the family of nuclear receptors.

A cDNA encoding a protein that binds retinoic acid with high affinity has been cloned. The protein is homologous to the receptors for steroid hormones, thyroid hormones and vitamin D3, and appears to be a retinoic acid-inducible trans-acting enhancer factor, suggesting that the molecular mechanisms of the effect of retinoids (vitamin A) on embryonic development, differentiation and tumour cell growth are similar to those described for other members of this nuclear receptor family.

Amino Acid Sequence↗