Two cellular retinoic acid binding proteins, CRABP I and II, which behaved differently on a DEAE-cellulose column, were purified from 14-day chick embryos. Their molecular weights were 15.8 kDa and 16.2 kDa, respectively. NH2-terminal 36 amino acid sequence of CRABP I was identical to that of bovine CRABP, which was reported previously. CRABP II was a novel cellular retinoic acid binding protein, in which the amino acids at 6 positions of the NH2 terminal sequence are different from those in CRABP I. The homology between CRABP I and II was more than 83%.
This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 16 February 1999.
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#12,344,996
of 34,363,559 outputs
Outputs from Biochemical & Biophysical Research Communications
#12,780
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#17,878
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Outputs of similar age from Biochemical & Biophysical Research Communications
#49
of 100 outputs
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