Molecular cloning of mouse mammary gland kappa-casein: comparison with rat kappa-casein and rat and human gamma-fibrinogen. 1985

M D Thompson, and J R Dave, and H L Nakhasi

A cDNA clone for kappa-casein mRNA from the lactating mouse mammary gland was isolated and its nucleotide sequence determined. Analysis of the deduced amino acid sequence revealed a precursor protein with a 21-amino-acid signal sequence and a mature protein of 160 amino acids, the mature mouse protein being 3 amino acids longer than the rat kappa-casein. Northern blot analysis of the lactating rat and mouse mammary gland showed a specific mRNA for rat kappa-casein and two distinct mRNAs for mouse kappa-casein. This result is explained by the presence of two putative polyadenylation sites in mouse kappa-casein cDNA, whereas rat kappa-casein cDNA has only one polyadenylation site. Comparison of the nucleotide sequence and of the deduced amino acid sequence of kappa-casein from mouse with that of the rat showed 85% homology between the two sequences. However, when amino acid sequences of kappa-casein from rat and mouse were compared with ovine kappa-casein, only a 45% homology was observed. Amino acid sequences of kappa-casein from rat, mouse, and sheep were 36.53% homologous with rat and human gamma-fibrinogen. The extent of homology was similar (32%) when nucleotide sequences of corresponding cDNAs were compared. The stretches of homology existing at different regions between the two proteins were more confined toward the amino-terminal half of gamma-fibrinogen. However, when nucleotide sequences were compared, mouse kappa-casein cDNA showed homology only with the second half of the rat gamma-fibrinogen cDNA, i.e., between nucleotides 661-1135. The homology with the human gamma-fibrinogen cDNA spanned over two regions, one between nucleotides 1-328 and the second between nucleotides 591-726.(ABSTRACT TRUNCATED AT 250 WORDS)

UI MeSH Term Description Entries
D011061 Poly A A group of adenine ribonucleotides in which the phosphate residues of each adenine ribonucleotide act as bridges in forming diester linkages between the ribose moieties. Adenine Polynucleotides,Polyadenylic Acids,Poly(rA),Polynucleotides, Adenine
D002364 Caseins A mixture of related phosphoproteins occurring in milk and cheese. The group is characterized as one of the most nutritive milk proteins, containing all of the common amino acids and rich in the essential ones. alpha-Casein,gamma-Casein,AD beta-Casein,Acetylated, Dephosphorylated beta-Casein,Casein,Casein A,K-Casein,Sodium Caseinate,alpha(S1)-Casein,alpha(S1)-Casein A,alpha(S1)-Casein B,alpha(S1)-Casein C,alpha(S2)-Casein,alpha-Caseins,beta-Casein,beta-Caseins,epsilon-Casein,gamma-Caseins,kappa-Casein,kappa-Caseins,AD beta Casein,Caseinate, Sodium,K Casein,alpha Casein,alpha Caseins,beta Casein,beta Caseins,beta-Casein Acetylated, Dephosphorylated,beta-Casein, AD,epsilon Casein,gamma Casein,gamma Caseins,kappa Casein,kappa Caseins
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning
D005260 Female Females
D005340 Fibrinogen Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products. Coagulation Factor I,Factor I,Blood Coagulation Factor I,gamma-Fibrinogen,Factor I, Coagulation,gamma Fibrinogen
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated

Related Publications

M D Thompson, and J R Dave, and H L Nakhasi
October 1978, Journal of molecular evolution,
M D Thompson, and J R Dave, and H L Nakhasi
March 1985, Cancer research,
M D Thompson, and J R Dave, and H L Nakhasi
January 1992, DNA sequence : the journal of DNA sequencing and mapping,
M D Thompson, and J R Dave, and H L Nakhasi
December 1984, The Journal of biological chemistry,
M D Thompson, and J R Dave, and H L Nakhasi
January 1988, Journal of dairy science,
M D Thompson, and J R Dave, and H L Nakhasi
February 1993, Zoological science,
M D Thompson, and J R Dave, and H L Nakhasi
February 1979, Biochimica et biophysica acta,
M D Thompson, and J R Dave, and H L Nakhasi
December 1979, Proceedings of the National Academy of Sciences of the United States of America,
M D Thompson, and J R Dave, and H L Nakhasi
January 2017, Methods in molecular biology (Clifton, N.J.),
M D Thompson, and J R Dave, and H L Nakhasi
January 1981, Journal of molecular evolution,
Copied contents to your clipboard!