Chemical Data on Pituitary Gonadotropins and Their Implication to Evolution

1982 ◽  
Vol 39 (1) ◽  
pp. 80-91 ◽  
Author(s):  
E. Burzawa-Gerard

Chemical data on gonadotropins from several vertebrate species are summarized and discussed from an evolutionary point of view. A high degree of homology has been observed between mammalian gonadotropins (LH and FSH) and thyrotropin (TSH). In non-mammalian species the existence of LH and FSH-like hormones has been demonstrated except for squamate and fish species. Especially in fish the number of GTHs is still controversial. One pituitary glycoprotein assumes various gonadotropic functions of the pituitary, and a second pituitary hormone (carbohydrate-poor) acts on fish ovarian growth. GTHs from bird, reptile, amphibian, and fish pituitaries have been purified and chemically characterized (amino acid composition, carbohydrate content). The existence of a quaternary structure has been demonstrated for several tetrapod LHs and fish GTHs. The amino acid composition of α and β subunits purified from turkey (Meleagris gallopavo), and turtle (Chelydra serpentira, Chelonia mydas) LHs and from common carp (Cyprinus carpio) and sturgeon (Acipenser stellatus) GTHs showed homology with the mammalian α and β subunits. The partial sequences of carp GTH subunits have shown that the carp GTH β was more closely related to mammalian LH β than to FSH β. Hybrid molecules could be obtained by association of heterologous subunits. The kinetics of subunit association has been studied in vitro. As compared to ovine LH, subunit association of carp GTH was more rapid and thermodependent. The subunit β seemed to determine the thermodependence. The various GTH subunits in living vertebrate probably derive from a common ancestral molecule.Key words: vertebrate gonadotropins, chemical characterizations, GTHs subunits, amino acid sequences, hybrid molecules, evolution.

1973 ◽  
Vol 133 (4) ◽  
pp. 805-819 ◽  
Author(s):  
Francesco Bossa ◽  
Donatella Barra ◽  
Massimo Carloni ◽  
Paolo Fasella ◽  
Francesca Riva ◽  
...  

Peptides produced by thermolytic digestion of aminoethylated aspartate aminotransferase and of the oxidized enzyme were isolated and their amino acid sequences determined. Digestion by elastase of the carboxymethylated enzyme gave peptides representing approximately 40% of the primary structure. Fragments from these digests overlapped with previously reported sequences of peptides obtained by peptic and tryptic digestion (Doonan et al., 1972), giving ten composite peptides containing 395 amino acid residues. The amino acid composition of these composite peptides agrees well with that of the intact enzyme. Confirmatory results for some of the present data have been deposited as Supplementary Publication 50018 at the National Lending Library for Science and Technology, Boston Spa, Yorks. LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1973) 131, 5.


1987 ◽  
Vol 248 (3) ◽  
pp. 933-936 ◽  
Author(s):  
I Sakai ◽  
F S Sharief ◽  
Y C Pan ◽  
S S Li

Human lactate dehydrogenase B (LDH-B) cDNA was isolated and sequenced. The LDH-B cDNA insert consists of the protein-coding sequence (999 bp), the 5′ (54 bp) and 3′ (203 bp) non-coding regions, and the poly(A) tail (50 bp). The predicted sequence of 333 amino acid residues was confirmed by amino acid composition and/or sequence analyses of a total of 185 (56%) residues from tryptic peptides of human LDH-B protein. The nucleotide and amino acid sequences of the human LDH-B coding region show 68% and 75% homologies respectively with those of the human LDH-A. The peptide map and amino acid composition data have been deposited as Supplementary Publication SUP 50139 (7 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment [see Biochem. J. (1987) 241, 5].


1971 ◽  
Vol 24 (2) ◽  
pp. 263 ◽  
Author(s):  
RJ Simpson ◽  
BE Davidson

Glyceraldehyde-3-phosphate dehydrogenase from leg muscle of M. rufa has been extracted and purified. The reaction of the enzyme with iodoacetate, the amino acid composition, tryptic fingerprint, and some amino acid sequences (in-cluding that around the reactive cysteine) indicate that kangaroo glyceraldehyde-3-phosphate dehydrogenase is almost identical with pig glyceraldehyde-3-phosphate dehydrogenase.


1984 ◽  
Vol 222 (1227) ◽  
pp. 259-271 ◽  

Peridinin-chlorophyll a -protein (PCP) complexes isolated from three strains of the symbiotic dinoflagellate Symbiodinium microadriaticum Freudenthal have been found to occur in multiple isoelectric forms, but the pattern of isoelectric forms of PCP is characteristic of each strain. Analysis of PCP after growth of the algae from Tridacna maxima, Cassiopeia frondosa, and Rhodactis sancti-thomae at 22, 57 and 157 μmol m -2 s -1 demonstrated that the patterns remained unchanged. Determination of the native molecular mass, quaternary structure and amino acid composition of two isoelectric forms of PCP derived from algae from Anthopleura elegantissima and Rhodactis sancti-thomae showed similar native molecular masses and amino acid composition, but while PCP from the algae from A. elegantissima is dimeric, PCP from algae from R. sancti-thomae is monomeric. The potential use of PCP as a taxonomic tool in dinoflagellate systematics and the evolution of multiple forms of these pigment-protein complexes are discussed.


1982 ◽  
Vol 2 (7) ◽  
pp. 503-508 ◽  
Author(s):  
Oi Tong Mak ◽  
Hans Jörnvall ◽  
Jonathan Jeffery

The native form of NAD-dependent 15-hydroxyprostaglandin dehydrogenase of human placenta has a mol. wt. of about 50 0002 while the subunit tool. wt. is around 2g 0002 suggesting a dimeric quaternary structure. These propertie% the amino acid composition, insensitivity to EDTA, and inhibition patterns show general similarities to other short-chain dehydrogenases. Several hormones tested did not influence the activity of 15-hydroxyprostaglandin dehydrogenase2 but an unusual activation by two anti-depressant drugs was found and may relate to the existence of a natural regulatory factor.


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