scholarly journals Snow Leopard (Panthera uncia ) Spermatozoa Are Sensitive to Alkaline pH, But Motility In Vitro Is Not Influenced by Protein or Energy Supplements

1996 ◽  
Vol 17 (5) ◽  
pp. 558-566 ◽  
Author(s):  
Terri L. Roth ◽  
William F. Swanson ◽  
Darin Collins ◽  
Michael Burton ◽  
Della M. Garell ◽  
...  
Reproduction ◽  
1994 ◽  
Vol 101 (3) ◽  
pp. 563-569 ◽  
Author(s):  
T. L. Roth ◽  
J. G. Howard ◽  
A. M. Donoghue ◽  
W. F. Swanson ◽  
D. E. Wildt
Keyword(s):  

2021 ◽  
Vol 30 (3) ◽  
pp. 797-817
Author(s):  
Charlotte E. Hacker ◽  
Matthew Jevit ◽  
Shafqat Hussain ◽  
Ghulam Muhammad ◽  
Bariushaa Munkhtsog ◽  
...  

PLoS ONE ◽  
2014 ◽  
Vol 9 (2) ◽  
pp. e88349 ◽  
Author(s):  
Salvador Lyngdoh ◽  
Shivam Shrotriya ◽  
Surendra P. Goyal ◽  
Hayley Clements ◽  
Matthew W. Hayward ◽  
...  

2020 ◽  
Vol 31 (3) ◽  
pp. 257-263
Author(s):  
Aline Laignier Soares-Yoshikawa ◽  
Jaime Aparecido Cury ◽  
Cínthia Pereira Machado Tabchoury

Abstract The aim of this in vitro study was to determine the fluoride concentration in silver diamine fluoride (SDF) products and their bioavailability with demineralized dentine. The products evaluated (expected fluoride concentrations) were: I: Saforide 38% (45,283 ppm F); II: Advantage Arrest 38.3 to 43.2% (45,283 to 51,013 ppm F); III: Ancárie 12% (14,100 ppm F); IV: Ancárie 30% (35,400 ppm F), V: Cariestop 12% (14,100 ppm F) and VI: Cariestop 30% (35,400 ppm F). The fluoride concentration was evaluated using an ion-specific electrode (ISE) by direct technique, which was confirmed after microdiffusion. The pH of the products was determined with a pH test strip. For the bioavailability test, demineralized dentine slabs were treated with one of the products for 1 min. Loosely (CaF2-like) and firmly-bound fluoride (FAp) were determined. The fluoride concentration found in the products (mean±SD; ppm F) by the ISE direct technique was: I:53,491±554; II:57,249±1,851; III:4,814±268; IV:5,726±43; V:10,145±468; VI:11,858±575; these values were confirmed after microdiffusion (t-test; p>0.05) and disagree with the declared by the manufacturers. The pH of Ancárie 12 and 30% was 6.0 and 4.5, respectively, in disagreement with the alkaline pH expected for SDF solution and found in the other products evaluated. There was no correlation between either CaF2-like (r=0.221; p=0.337) or FAp (r=-0.144; p=0.830) formed in demineralized dentine and fluoride concentration found in the products. The problems of pH and fluoride concentration found in available professional commercial SDF products suggest that they are not under sanitary surveillance.


PLoS ONE ◽  
2012 ◽  
Vol 7 (2) ◽  
pp. e32104 ◽  
Author(s):  
Wasim Shehzad ◽  
Thomas Michael McCarthy ◽  
Francois Pompanon ◽  
Lkhagvajav Purevjav ◽  
Eric Coissac ◽  
...  

1992 ◽  
Vol 103 (3) ◽  
pp. 709-718 ◽  
Author(s):  
M. Brunkener ◽  
S.D. Georgatos

Filensin is a 100/110 kDa membrane-associated protein found in lens fiber cells. Previous studies have shown that this protein polymerizes in vitro and binds strongly to vimentin and to another 47 kDa lens membrane protein. Using cosedimentation assays, flotation assays and immunoelectron microscopy, we have examined the properties of purified filensin and measured its binding to lens membranes. Filensin behaves as a ureaextractable, hydrophilic protein which does not partition with Triton X-114 and is not affected by 1 M hydroxylamine at alkaline pH, an agent known to release fatty-acylated proteins from the membrane. Immunoblotting of urea-extracted lens membranes with two different affinity-purified antibodies reveals that, unlike intact filensin, a COOH-terminal filensin degradation product (51 kDa) remains tightly associated with the membranes. Purified filensin binds directly to urea-stripped lens membranes, but not to protein-free vesicles reconstituted from total lens lipids. The binding of filensin is not significantly influenced by the purified 47 kDa protein. Interestingly, the filensin-binding capacity of urea-extracted membranes is increased at least two-fold after trypsin treatment, which removes entirely the 51 kDa peptide from the membranes and presumably unmasks additional filensin-acceptor sites. Consistent with this, filensin binds to trypsinized and non-trypsinized membranes with similar affinities (2 × 10(−7) and 4 × 10(−7) M, respectively). Treatment of the membranes with thrombin, which also eliminates the 51 kDa peptide, does not increase their binding capacity, apparently because filensin-acceptor sites are also destroyed during proteolysis.(ABSTRACT TRUNCATED AT 250 WORDS)


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