Gliding Motility of Mycoplasma mobile Can Occur by Repeated Binding to N-Acetylneuraminyllactose (Sialyllactose) Fixed on Solid Surfaces

ABSTRACT Mycoplasma mobile relies on an unknown mechanism to glide across solid surfaces including glass, animal cells, and plastics. To identify the direct binding target, we examined the factors that affect the binding of Mycoplasma pneumoniae to solid surfaces and concluded that N-acetylneuraminyllactose (sialyllactose) attached to a protein can mediate glass binding on the basis of the following four lines of evidence: (i) glass binding was inhibited by N-acetylneuraminidase, (ii) glass binding was inhibited by N-acetylneuraminyllactose in a structure-dependent manner, (iii) binding occurred on glass pretreated with bovine serum albumin attached to N-acetylneuraminyllactose, and (iv) gliding speed depended on the density of N-acetylneuraminyllactose on glass.

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Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation

Development ◽

10.1242/dev.121.4.1129 ◽

1995 ◽

Vol 121 (4) ◽

pp. 1129-1137 ◽

Cited By ~ 6

Author(s):

P.E. Visconti ◽

J.L. Bailey ◽

G.D. Moore ◽

D. Pan ◽

P. Olds-Clarke ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Tyrosine Phosphorylation ◽

Bovine Serum ◽

Female Reproductive Tract ◽

Dependent Manner ◽

Protein Tyrosine Phosphorylation ◽

Sperm Capacitation ◽

Protein Tyrosine

The molecular basis of mammalian sperm capacitation, defined functionally as those processes that confer on the sperm the acquisition of fertilization-competence either in vivo in the female reproductive tract or in vitro, is poorly understood. We demonstrate here that capacitation of caudal epididymal mouse sperm in vitro is accompanied by a time-dependent increase in the protein tyrosine phosphorylation of a subset of proteins of M(r) 40,000-120,000. Incubation of sperm in media devoid of bovine serum albumin, CaCl2 or NaHCO3, components which individually are required for capacitation, prevent the sperm from undergoing capacitation as assessed by the ability of the cells to acquire the pattern B chlortetracycline fluorescence, to undergo the zona pellucida-induced acrosome reaction and, in some cases, to fertilize metaphase II-arrested eggs in vitro. In each of these cases the protein tyrosine phosphorylation of the subset of capacitation-associated proteins does not occur. Protein tyrosine phosphorylation of these particular proteins, as well as sperm capacitation, can be recovered in media devoid of each of these three constituents (bovine serum albumin, CaCl2 or NaHCO3) by adding back the appropriate component in a concentration-dependent manner. The requirement of NaHCO3 for these phosphorylations is not due to an alkalinization of intracellular sperm pH or to an increase in media pH. Caput epididymal sperm, which lack the ability to undergo capacitation in vitro, do not display this capacitation-dependent subset of tyrosine phosphorylated proteins in complete media even after extended incubation periods, and do not fertilize metaphase II-arrested eggs in vitro.(ABSTRACT TRUNCATED AT 250 WORDS)

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Bovine serum albumin adsorption and desorption rates on solid surfaces with varying surface properties

Journal of Colloid and Interface Science ◽

10.1016/0021-9797(87)90450-4 ◽

1987 ◽

Vol 118 (1) ◽

pp. 212-223 ◽

Cited By ~ 49

Author(s):

Yu Ling Cheng ◽

Seth A. Darst ◽

Channing R. Robertson

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Surface Properties ◽

Bovine Serum ◽

Solid Surfaces ◽

Adsorption And Desorption ◽

Bovine Serum Albumin Adsorption ◽

Albumin Adsorption

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β-glucan: Immune boosting potential and antioxidant candidate

International Journal of Research in Pharmaceutical Sciences ◽

10.26452/ijrps.v11i1.1849 ◽

2020 ◽

Vol 11 (1) ◽

pp. 491-496

Author(s):

Abhishek Kamboj ◽

Aanchal Jain ◽

Tanya Singh ◽

Ajam Shaikh ◽

Amit Gupta

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Specific Protein ◽

Antioxidant Potential ◽

Cell Culture Supernatant ◽

Dependent Manner ◽

Dpph Assay ◽

Concentration Dependent Manner ◽

Ifn Gamma

In literature, β-glucan is abundantly found in oats and currently used as well as tested against various varieties of food products. The objective of our study is to evaluate its immune-boosting potential of β-glucan extracted from oats and tested against specific protein antigen i.e., bovine serum albumin (BSA) and also measure its antioxidant activity. For these studies, β-glucan using variable concentration and tested in human whole blood samples (exposed with an optimized concentration of bovine serum albumin, BSA) and examined its immune-boosting potential. In contrast, estimation of Th1 (IFN-gamma) and Th2 (IL-4) cytokines were also measured from cell culture supernatant and also measured its antioxidant potential through DPPH assay. The results showed that β-glucan enhanced immune-boosting activity in a concentration-dependent manner against BSA. In contrast, there is enhancement in Th2 (IL-4) cytokines in a dose-dependent manner, but there is no significant effect in Th1 (IFN-gamma) as compared to control. In addition, β-glucan showed drastic enhanced antioxidant potential, which is confirmed through DPPH assay. The data demonstrate that β-glucan showing immune-boosting properties and antioxidant potential.

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Applicability of the extended Derjaguin–Landau–Verwey–Overbeek theory on the adsorption of bovine serum albumin on solid surfaces

Biointerphases ◽

10.1116/1.4904074 ◽

2014 ◽

Vol 9 (4) ◽

pp. 041006 ◽

Cited By ~ 7

Author(s):

Hua Wang ◽

Bi-min Zhang Newby

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Solid Surfaces

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Does the anesthetic 2,2,2-trifluoroethanol interact with bovine serum albumin by direct binding or by solvent-mediated effects? A calorimetric and spectroscopic investigation

Biopolymers ◽

10.1002/bip.20262 ◽

2005 ◽

Vol 78 (2) ◽

pp. 78-86 ◽

Cited By ~ 19

Author(s):

Tuhina Banerjee ◽

Nand Kishore

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Spectroscopic Investigation ◽

Bovine Serum ◽

Mediated Effects ◽

Direct Binding

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Evaluation of in vitro anti-inflammatory activity of the spadix of Colocasia affinis

Science Vision ◽

10.33493/scivis.19.02.06 ◽

2019 ◽

Vol 19 (2) ◽

pp. 30-34

Author(s):

Vanlalhruaii ◽

C. Malsawmtluangi ◽

H. Lalhlenmawia

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Bovine Serum ◽

Methanolic Extract ◽

Inflammatory Activity ◽

Dependent Manner ◽

Protease Inhibition ◽

Egg Albumin ◽

Anti Inflammatory

The methanolic extract of C. affinis was evaluated for its in-vitro anti-inflammatory activity by bovine serum albumin denaturation method, egg albumin denaturation method and protease inhibition method at different concentrations. Diclofenac sodium was used as the reference drug. The extract exhibits anti-inflammatory activity in a concentration-dependent manner. In bovine serum albumin denaturation method, the extract at concentrations of 100, 200, 400, 600, 800, 1000 µg/ml showed 25.49, 28.43, 31.37, 37.25, 41.17, 48.03% inhibition respectively. In egg albumin denaturation method, the concentrations of 50, 100, 200, 300, 400, 500 µg/ml showed 5.3, 9.89, 28.12, 32.8, 43.2, 52.8% inhibition respectively. In protease inhibition method the extract at concentration of 100, 200, 300, 400, 500 µg/ml showed 8.87, 19.32, 28.56, 43.96, 59.92% inhibition respectively. Therefore, from the results it can be concluded that the methanolic extract of C. affinis possesses anti-inflammatory activity.

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Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway

Development ◽

10.1242/dev.121.4.1139 ◽

1995 ◽

Vol 121 (4) ◽

pp. 1139-1150 ◽

Cited By ~ 35

Author(s):

P.E. Visconti ◽

G.D. Moore ◽

J.L. Bailey ◽

P. Leclerc ◽

S.A. Connors ◽

...

Keyword(s):

Bovine Serum Albumin ◽

Serum Albumin ◽

Tyrosine Phosphorylation ◽

Bovine Serum ◽

Biologically Active ◽

Dependent Manner ◽

Protein Tyrosine Phosphorylation ◽

Concentration Dependent Manner ◽

Mouse Sperm ◽

Protein Tyrosine

In the accompanying report (Visconti, P.E., Bailey, J.L., Moore, G.D., Pan, D., Olds-Clarke, P. and Kopf, G.S. (1995) Development, 121, 1129–1137) we demonstrated that the tyrosine phosphorylation of a subset of mouse sperm proteins of M(r) 40,000-120,000 was correlated with the capacitation state of the sperm. The mechanism by which protein tyrosine phosphorylation is regulated in sperm during this process is the subject of this report. Cauda epididymal sperm, when incubated in media devoid of NaHCO3, CaCl2 or bovine serum albumin do not display the capacitation-associated increases in protein tyrosine phosphorylation of this subset of proteins. This NaHCO3, CaCl2 or bovine serum albumin requirement for protein tyrosine phosphorylation can be completely overcome by the addition of biologically active, but not inactive, cAMP analogues. Addition of the active cAMP analogues to sperm incubated in media devoid of NaHCO3, CaCl2 or bovine serum albumin overcomes the inability of these media to support capacitation, as assessed by the ability of the cells to acquire the pattern B chlortetracycline fluorescence, to undergo the zona pellucida-induced acrosome reaction and, in some cases, to fertilize metaphase II-arrested eggs in vitro. The effects of the cAMP analogues to enhance protein tyrosine phosphorylation and to promote capacitation appears to be at the level of the cAMP-dependent protein kinase (PKA), since two specific inhibitors of this enzyme (H-89 and Rp-cAMPS) block the capacitation-dependent increases in protein tyrosine phosphorylation in sperm incubated in media supporting capacitation. Capacitation, as assessed by the aforementioned endpoints, also appears to be inhibited by H-89 in a concentration-dependent manner. These results provide further evidence for the interrelationship between protein tyrosine phosphorylation and the appearance of the capacitated state in mouse sperm. They also demonstrate that both protein tyrosine phosphorylation and capacitation appear to be regulated by cAMP/PKA. Up-regulation of protein tyrosine phosphorylation by cAMP/PKA in sperm is, to our knowledge, the first demonstration of such an interrelationship between tyrosine kinase/phosphatase and PKA signaling pathways.

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