High impact information on csn1s1

• Transcription of the alpha s1-casein gene is induced by PRL [1].
• The relative abundance of alpha-S1-casein, beta-lactoglobulin, and alpha-lactalbumin mRNAs similarly decline between 8 and 24 h in culture [2].
• Genetic variants A and D of bovine alpha s2-casein, beta-casein variants A1, A2, A3, B and C and alpha s1-casein variants B and C were determined by CE [3].
• Expression patterns of alpha-S1-casein were similar to those of alpha-lactalbumin [4].
• Moreover, significant irreversible binding occurred when the cysteine free protein, alpha s1-casein, was incubated in solution with zomepirac glucuronide in vitro [5].

Biological context of csn1s1

• The nucleotide sequence of alpha s1-casein mRNA was determined by sequencing, according to Maxam and Gilbert, both a 1080 bp long cloned ds-cDNA and a ss-cDNA (268 nucleotides) generated by 5' extension of a 5' terminal truncated radiolabeled fragment (83 bp) of the relevant ds-cDNA, used as primer for reverse transcription [6].
• The derived 206 amino acid sequence of ovine pre-alpha s1-casein differs from that of its bovine counterpart (genetic variant B) by 24 amino acid substitutions and a deletion of 8 amino acid residues occurring in the polypeptide chain of the mature protein [6].
• A cooperation between distal and proximal regions of the alpha s1-casein gene is responsible for the PRL-dependent enhancer activity of the distal fragment [1].
• Effects of sheep alpha s1-casein CC, CD and DD genotypes on milk composition and cheesemaking properties [7].
• Both two dimensional electrophoresis followed by staining with polyclonal antibodies against alpha s1-casein and electrospray mass spectrometry showed a heterogeneity consistent with that expected from a protein chain with three levels of phosphorylation and two different lengths [8].

Associations of csn1s1 with chemical compounds

• The 199 residue peptide chain, which accounted for approximately 80% of the entire translated alpha s1-casein, was as long as its caprine and bovine counterparts, and had a 98 and 89% degree of identity with those two proteins respectively [9].
• Nine serine residues (positions 12, 44, 46, 64 to 68 and 75) were fully phosphorylated in alpha s1-casein A, whereas Ser115 and Ser41 were phosphorylated by approximately 50 and approximately 20% respectively [9].
• Most of the peptides originated from alpha s1-casein (CN), especially from the N-terminal half of the molecule [10].

Analytical, diagnostic and therapeutic context of csn1s1

• Gel isoelectric focusing and electrospray mass spectrometry were used to demonstrate that the first HPLC peak contained the 191 residue alpha s1-casein molecular species and the second the 199 residue species, in proportions of approximately 20:80 [8].

References