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At least 253 records · Page 14Linked to original sources
PubMed1980

[Morphologic evolution of the human extensor digitorum and the abductor pollicis longus muscles. II. Morphologic evolution of the human extensor digiti minimi, the abductor pollicis longus, the extensor pollicis brevis and the extensor pollicis longus muscles].

The author has studied the macroscopic morphology of the above mentioned muscles over 3 groups of material: 1. 200 superior limbs of adults and 100 superior limbs of human foetuses from 4,8 cm to 37 cm C.H.L. 2. 100 thoracic limbs from 25 species of non-hominid Primates, 13 thoracic limbs from 6 species of Marsupials and 9 thoracic limbs from 2 species of Insectivores. 3. The organogenesis of the muscles in question is studied over the complete series of transversal cuts of 18 superior limbs of human embryos and foetuses from 13,5 mm to 60 mm C.H.L. Comparison and discussion of the facts is made according to the principles of the evolutionary myology.

Animals↗
PubMed1995

Band 3, the anion transporter, is conserved during evolution: implications for aging and vertebrate evolution.

A cDNA fragment corresponding to a highly evolutionarily conserved region of the major anion transport protein band 3 was cloned from lamprey mRNA using PCR homology probing. This is the first report providing evidence for a band-3 like transporter in the lowest vertebrates, the agnathostomes. Semi-quantitative PCR showed expression similar to that of higher vertebrates. Lamprey serum contains antibody-like molecules that bind to synthetic peptides of band 3 comprising senescent cell antigen, an aging antigen that terminates the life of cells. The high degree of homology found in nucleic acid and derived proteins sequence and the reaction of "antibodies" in lamprey serum with senescent cell antigen peptides of band 3 suggests that lamprey band 3 plays a role comparable to that in higher vertebrates.

Aging↗
PubMed1972

Evolution of neurophysin proteins: the partial sequence of bovine neurophysin-I (vasopressin-oxytocin-carrier proteins-automated amino-acid-sequence analysis-homology-protein evolution).

The sequence of the first 50 amino-acid residues of bovine neurophysin-I was determined. A comparison of this sequence with that of the 97-residue bovine neurophysin-II and the 92-residue porcine neurophysin-I molecules reveals a high degree of homology among these proteins. It is suggested that the binding site of neurophysin proteins for neurohypophyseal hormones is located in the middle portion of these molecules, where their sequences are virtually identical. The sequence data, as well as the occurrence of at least two neurophysins in both the pig and the cow, suggest that each species inherited at least two structural genes controlling the synthesis of these proteins. The most striking finding in the study was the observation of internal sequence homologies within the neurophysins. This result implies that these molecules arose by way of a series of partial gene duplications of a primitive gene that coded for a smaller ancestral protein.

Acetamides↗