Rat alpha-lactalbumin has a 17-residue-long COOH-terminal hydrophobic extension as judged by sequence analysis of the cDNA clones.
- 1 August 1981
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 78 (8) , 4853-4857
- https://doi.org/10.1073/pnas.78.8.4853
Abstract
Complementary(c)DNA for rat mammary gland .alpha.-lactalbumin was cloned in a bacterial plasmid, and its sequence was analyzed. The DNA sequence analysis shows that rat .alpha.-lactalbumin has 17 extra residues beyond the COOH terminus of the .alpha.-lactalbumin isolated and sequenced to date from other species. The predicted COOH-terminal sequence is hydrophobic and proline rich and bears some resemblance to .beta.-casein sequences.This publication has 34 references indexed in Scilit:
- Inverted terminal repetition in vaccinia virus DNA encodes early mRNAsNature, 1980
- Involvement of histidine-32 in the biological activity of .alpha.-lactalbuminBiochemistry, 1979
- 3′ Non-coding region sequences in eukaryotic messenger RNANature, 1976
- An Efficient mRNA‐Dependent Translation System from Reticulocyte LysatesEuropean Journal of Biochemistry, 1976
- Genetic studies with heteroduplex DNA of bacteriophage f1. Asymmetric segregation, base correction and implications for the mechanism of genetic recombinationJournal of Molecular Biology, 1975
- Lactose biosynthesisPublished by Springer Nature ,1975
- Lactose SynthetasePublished by Wiley ,1975
- The Complete Amino-Acid Sequence of Guinea-Pig alpha-LactalbuminEuropean Journal of Biochemistry, 1972
- The Complete Amino‐Acid Sequence of Human α‐LactalbuminEuropean Journal of Biochemistry, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970