ADULT ERYOPS, LARGEST SEMI-AQUATIC APEX PREDATORS OF THE TEXAS RED BEDS, LOWER CLEAR FORK, PREFERRED FAST FLOWING STREAMS, PREYING UPON EDAPHOSAURS, DIMETRODONTS AND OTHER ERYOPS

2019 ◽  
Author(s):  
Chris J. Flis ◽  
◽  
Robert T. Bakker ◽  
James E. Flis ◽  
Mallori M. Hass ◽  
...  
Keyword(s):  
Red Beds ◽  
1942 ◽  
Vol 50 (8) ◽  
pp. 925-960 ◽  
Author(s):  
Alfred S. Romer ◽  
Robert V. Witter
Keyword(s):  
Red Beds ◽  

2018 ◽  
Vol 92 (6) ◽  
pp. 1092-1106
Author(s):  
Bryan M. Gee ◽  
Steven J. Rosscoe ◽  
Diane Scott ◽  
Judie Ostlien ◽  
Robert R. Reisz

AbstractThe Texas red beds represent one of the richest series of early Permian deposits in the world. In particular, the Clear Fork Group has produced a diverse assemblage of temnospondyls, early reptiles, and synapsids. However, most of this material has been sourced from the oldest member, the Arroyo Formation, and the understanding of the paleoecosystem of the younger Vale and Choza formations is less well resolved. Here we present a previously undescribed Vale locality, the first vertebrate-bearing locality from the formation to be described in detail in several decades, from near Abilene, Texas with juvenile diplocaulids, captorhinids, abundant material of rare taxa such asVaranopsand diadectids, and the first report of a recumbirostran ‘microsaur’ from the formation. This assemblage is atypical of early Permian deposits in the taxonomic and size distribution of the vertebrate fauna in comparison to other localities from the Vale Formation that preserve a greater abundance of aquatic taxa (e.g., fishes,Trimerorhachis) and synapsids (e.g.,Dimetrodon). Minimal abrasion of the elements, relative articulation and association of the specimen ofVaranops, and the paucity of aquatic taxa suggest an ephemeral pond deposit in which organisms were preserved essentially in situ. Our characterization of the locality also permits a revision and discussion of the vertebrate faunal assemblage of the Vale Formation.


Author(s):  
Barbara Trask ◽  
Susan Allen ◽  
Anne Bergmann ◽  
Mari Christensen ◽  
Anne Fertitta ◽  
...  

Using fluorescence in situ hybridization (FISH), the positions of DNA sequences can be discretely marked with a fluorescent spot. The efficiency of marking DNA sequences of the size cloned in cosmids is 90-95%, and the fluorescent spots produced after FISH are ≈0.3 μm in diameter. Sites of two sequences can be distinguished using two-color FISH. Different reporter molecules, such as biotin or digoxigenin, are incorporated into DNA sequence probes by nick translation. These reporter molecules are labeled after hybridization with different fluorochromes, e.g., FITC and Texas Red. The development of dual band pass filters (Chromatechnology) allows these fluorochromes to be photographed simultaneously without registration shift.


Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.


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