Isolation and biochemical characterization of heparin-binding proteins from boar seminal plasma: A dual role for spermadhesins in fertilization

1993 ◽  
Vol 35 (1) ◽  
pp. 37-43 ◽  
Author(s):  
Libia Sanz ◽  
Juan J. Calvete ◽  
Karlheinz Mann ◽  
Hans-Joachim Gabius ◽  
Edda Töpfer-Petersen
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Biochemical Characterization ◽  
Dual Role ◽  
Heparin Binding

scholarly journals Proteins of the canine seminal plasma

2016 ◽  
Vol 46 (5) ◽  
pp. 901-908 ◽  
Author(s):  
Annice Aquino-Cortez ◽  
Lúcia Daniel Machado da Silva ◽  
Airton Alencar de Araújo ◽  
Erika da Silva Bezerra de Menezes ◽  
Arlindo de Alencar Araripe Noronha Moura
Keyword(s):  
Alkaline Phosphatase ◽  
Seminal Plasma ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Sperm Quality ◽  
Zinc Binding ◽  
Heparin Binding ◽  
Reproductive Disorders ◽  
The Matrix ◽  
Peroxidase Enzymes

ABSTRACT: Studies have been performed to identify the proteins present in canine seminal plasma (SP) and relate them to sperm quality as well as to discover molecular markers of reproductive tract diseases. There is evidence that heparin-binding proteins, zinc-binding proteins, and lactoferrin as well as the matrix metalloproteinase, superoxide dismutase, catalase, and glutathione peroxidase enzymes are associated with canine sperm quality. Other studies indicate that prolactin and enzymes like arginine esterase, acid phosphatase, and alkaline phosphatase could be successfully used as biomarkers of reproductive disorders. Thus, the present literature review aims to address aspects related to proteins of the canine SP, their influence on fertility, and their importance as biomarkers of reproductive disorders.

scholarly journals Heparin-binding proteins of canine seminal plasma

2006 ◽  
Vol 66 (6-7) ◽  
pp. 1606-1609 ◽  
Author(s):  
Fabiana Ferreira de Souza ◽  
Maria Isabel Mello Martins ◽  
Carlos Eurico dos Santos Fernandes ◽  
Paulo Eduardo Martins Ribolla ◽  
Maria Denise Lopes
Keyword(s):  
Seminal Plasma ◽  
Binding Proteins ◽  
Heparin Binding

In Vitro Biochemical Characterization of Cytokinesis Actin-Binding Proteins

2016 ◽  
pp. 151-179 ◽  
Author(s):  
Dennis Zimmermann ◽  
Alisha N. Morganthaler ◽  
David R. Kovar ◽  
Cristian Suarez
Keyword(s):  
Binding Proteins ◽  
Biochemical Characterization ◽  
Actin Binding ◽  
Actin Binding Proteins

scholarly journals Heparin- and Zn2+-binding proteins from boar seminal plasma.

1999 ◽  
Vol 46 (4) ◽  
pp. 935-939 ◽  
Author(s):  
D Hołody ◽  
J Strzezek
Keyword(s):  
Amino Acid ◽  
Affinity Chromatography ◽  
Molecular Mass ◽  
Seminal Plasma ◽  
Binding Proteins ◽  
Reproductive Tract ◽  
Female Reproductive Tract ◽  
Heparin Binding ◽  
Sds Page ◽  
Protein Components

Low molecular mass, heparin-binding proteins from seminal plasma play an important role in gametes interaction whereas plasmatic Zn2+-binding proteins stabilize chromatin and plasmalemma structures and protect spermatozoa in the female reproductive tract. By means of affinity chromatography the heparin- and Zn2+-binding proteins were isolated from boar seminal plasma and both preparations were analyzed by reverse HPLC. Most of the proteins bound to heparine and Zn2+-ions were classified as spermadhesins. Three fractions binding exclusively Zn2+ were isolated. They differ in amino-acid composition, content of glucosamine and content of protein components revealed by SDS/PAGE.

scholarly journals Evidence for an Elongated Dimeric Structure of Heparin-Binding Hemagglutinin from Mycobacterium tuberculosis

2008 ◽  
Vol 190 (13) ◽  
pp. 4749-4753 ◽  
Author(s):  
Carla Esposito ◽  
Maxim V. Pethoukov ◽  
Dmitri I. Svergun ◽  
Alessia Ruggiero ◽  
Carlo Pedone ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Virulence Factor ◽  
Biochemical Characterization ◽  
Coiled Coil ◽  
Heparin Binding ◽  
Truncated Form ◽  
X Ray ◽  
Dimeric Structure ◽  
X Ray Scattering

ABSTRACT Heparin-binding hemagglutinin (HBHA) is a virulence factor of tuberculosis which is responsible for extrapulmonary dissemination of this disease. A thorough biochemical characterization of HBHA has provided experimental evidence of a coiled-coil nature of HBHA. These data, together with the low-resolution structures of a full-length form and a truncated form of HBHA obtained by small-angle X-ray scattering, have unambiguously indicated that HBHA has a dimeric structure with an elongated shape.

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