| |
|
|
 | Acesso ao texto completo restrito à biblioteca da Embrapa Caprinos e Ovinos. Para informações adicionais entre em contato com cnpc.biblioteca@embrapa.br. |
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Caprinos e Ovinos. |
|
Data corrente: |
01/08/1992 |
|
Data da última atualização: |
26/04/2023 |
|
Autoria: |
IRITANI, A.; NISHIKAWA, Y. |
|
Afiliação: |
Lab. of Animal Reprod., College of Agric., Kyoto Univ.; Lab. of Animal Reprod., College of Agric., Kyoto Univ. |
|
Título: |
Studies on the egg yolk-coagulating enzyme in goat semen. V. Purification of the egg yolk coagulating enzyme. |
|
Ano de publicação: |
1963 |
|
Fonte/Imprenta: |
Japanese Journal of Animal Reproduction, v. 8, n. 4, p. 118-121, 1963. |
|
DOI: |
https://doi.org/10.1262/jrd1955.8.118 |
|
Idioma: |
Japonês |
|
Conteúdo: |
Abstract: Existence of the egg yolk-coagulating enzyme in goat semen was found recently, yet its purificationhas not been attempted. While it is generally very important and significant to extract an enzyme inthe purified state in order to clarify the characteristics especially for those discovered such as the onediscussed here. In this experiment, the authors tried to purify the enzyme by the following methods; salting out byammonium sulfate, selecting adsorbtion with tricalcium phosphate-gel, andthe acetone fractionation. Principal results obtained were as follows. 1. Selecting precipitation method with ammonium sulfate was tried on the goat seminal plasma toobtain the enzyme rich fraction, but most ofthe seminal plasma protein was abruptly salted out ataround 30%ammonium sulfate. And it was difficult to extract the enzyme rich fraction by this method. 2. Then the selecting adsorbtion method was performed. Seminal plasma protein was salted out adding equal volume of saturated ammonium sulfate, and dialized the precipitated protein for 12 hours at 4°C, then it was adsorbed to the tricalcium phosphate-gel, and the selecting elution was made addingvarious concentrations of the phosphate buffer to the protein adsorbed calcium-gel. As the results, considerably purified enzyme was obtained from the fraction eluted into 0.25 M phoshate buffer. Besides, the purity of the enzyme in this fraction was about 10 times higher than that of the starting material, seminal plasma. 3. Purification of the coagulating enzyme was performed by the acetone fractionation starting from the goat seminal plasma. Acetone was added to the goat seminal plasma to be 33%, 45%, 51%, 62.%, 67%, and 77% of the concentration in the mixture at 0°C, then each of the precipitated fraction wasobtained after ultracentrifugation. Thus, it was confirmed that the fraction precipitated at the concentration of 33%acetone shows the highest apecific scivity, and the purity of the enzyme was about 4 times higher than that of the starting materia1, goat seminal plasma. Furthermore, paperelectrophoretic studies were performed on each of the fraction obtained above. Andit was clarified that the enzyme-rich fraction shows low mobility, and the remaining 4 fractions free from most of the enzyme have high mobility. MenosAbstract: Existence of the egg yolk-coagulating enzyme in goat semen was found recently, yet its purificationhas not been attempted. While it is generally very important and significant to extract an enzyme inthe purified state in order to clarify the characteristics especially for those discovered such as the onediscussed here. In this experiment, the authors tried to purify the enzyme by the following methods; salting out byammonium sulfate, selecting adsorbtion with tricalcium phosphate-gel, andthe acetone fractionation. Principal results obtained were as follows. 1. Selecting precipitation method with ammonium sulfate was tried on the goat seminal plasma toobtain the enzyme rich fraction, but most ofthe seminal plasma protein was abruptly salted out ataround 30%ammonium sulfate. And it was difficult to extract the enzyme rich fraction by this method. 2. Then the selecting adsorbtion method was performed. Seminal plasma protein was salted out adding equal volume of saturated ammonium sulfate, and dialized the precipitated protein for 12 hours at 4°C, then it was adsorbed to the tricalcium phosphate-gel, and the selecting elution was made addingvarious concentrations of the phosphate buffer to the protein adsorbed calcium-gel. As the results, considerably purified enzyme was obtained from the fraction eluted into 0.25 M phoshate buffer. Besides, the purity of the enzyme in this fraction was about 10 times higher than that of the starting material, seminal plasma. 3. Purifi... Mostrar Tudo |
|
Thesagro: |
Bioquímica; Caprino; Coagulação; Enzima; Reprodução; Sêmen. |
|
Thesaurus Nal: |
Animal reproduction; Egg yolk; Enzymes; Goats. |
|
Categoria do assunto: |
L Ciência Animal e Produtos de Origem Animal |
|
Marc: |
LEADER 03080naa a2200265 a 4500
001 1523734
005 2023-04-26
008 1963 bl uuuu u00u1 u #d
024 7 $ahttps://doi.org/10.1262/jrd1955.8.118$2DOI
100 1 $aIRITANI, A.
245 $aStudies on the egg yolk-coagulating enzyme in goat semen. V. Purification of the egg yolk coagulating enzyme.$h[electronic resource]
260 $c1963
520 $aAbstract: Existence of the egg yolk-coagulating enzyme in goat semen was found recently, yet its purificationhas not been attempted. While it is generally very important and significant to extract an enzyme inthe purified state in order to clarify the characteristics especially for those discovered such as the onediscussed here. In this experiment, the authors tried to purify the enzyme by the following methods; salting out byammonium sulfate, selecting adsorbtion with tricalcium phosphate-gel, andthe acetone fractionation. Principal results obtained were as follows. 1. Selecting precipitation method with ammonium sulfate was tried on the goat seminal plasma toobtain the enzyme rich fraction, but most ofthe seminal plasma protein was abruptly salted out ataround 30%ammonium sulfate. And it was difficult to extract the enzyme rich fraction by this method. 2. Then the selecting adsorbtion method was performed. Seminal plasma protein was salted out adding equal volume of saturated ammonium sulfate, and dialized the precipitated protein for 12 hours at 4°C, then it was adsorbed to the tricalcium phosphate-gel, and the selecting elution was made addingvarious concentrations of the phosphate buffer to the protein adsorbed calcium-gel. As the results, considerably purified enzyme was obtained from the fraction eluted into 0.25 M phoshate buffer. Besides, the purity of the enzyme in this fraction was about 10 times higher than that of the starting material, seminal plasma. 3. Purification of the coagulating enzyme was performed by the acetone fractionation starting from the goat seminal plasma. Acetone was added to the goat seminal plasma to be 33%, 45%, 51%, 62.%, 67%, and 77% of the concentration in the mixture at 0°C, then each of the precipitated fraction wasobtained after ultracentrifugation. Thus, it was confirmed that the fraction precipitated at the concentration of 33%acetone shows the highest apecific scivity, and the purity of the enzyme was about 4 times higher than that of the starting materia1, goat seminal plasma. Furthermore, paperelectrophoretic studies were performed on each of the fraction obtained above. Andit was clarified that the enzyme-rich fraction shows low mobility, and the remaining 4 fractions free from most of the enzyme have high mobility.
650 $aAnimal reproduction
650 $aEgg yolk
650 $aEnzymes
650 $aGoats
650 $aBioquímica
650 $aCaprino
650 $aCoagulação
650 $aEnzima
650 $aReprodução
650 $aSêmen
700 1 $aNISHIKAWA, Y.
773 $tJapanese Journal of Animal Reproduction$gv. 8, n. 4, p. 118-121, 1963.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Caprinos e Ovinos (CNPC) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
| Registros recuperados : 11 | |
| 1. |  | ACCIOLY, L. J. de O.; HUETE, A. R. Resposta espectral de solos em razão do ângulo de visada, da umidade e da rugosidade superficial. Pesquisa Agropecuária Brasileira, Brasília, DF, v. 35, n. 12, p. 2473-84, dez. 2000. Título em inglês: Soil spectral response in relation to viewing angle, soil moisture and surface roughness.| Tipo: Artigo em Periódico Indexado |
| Biblioteca(s): Embrapa Solos; Embrapa Unidades Centrais. |
|    |
| 5. | | MIURA, T.; HUETE, A. R.; FERREIRA, L. G.; SANO, E. E. An assessment of land cover dependencies of VI-biophysical relationships for regional extrapolations of ground LBA ecology measurements in Brazilian Cerrado. In: CONFERÊNCIA CIENTÍFICA DO LBA, 3., 2004, Brasília, DF. Anais de trabalhos completos. Brasília, DF: LBA, 2004. 1 p.| Biblioteca(s): Embrapa Cerrados. |
| |
| 7. | | SANO, E. E.; HUETE, A. R.; TROUFLEAU, D.; MORAN, M. S.; VIDAL, A. Relation between ERS-1 synthetic aperture radar data and measurements of surface roughness and moisture content of rocky soils in a semiarid rangeland. Water Resources Research, Washington, v. 34, n. 6, p. 1491-1498, 1998.| Tipo: Artigo em Periódico Indexado |
| Biblioteca(s): Embrapa Cerrados. |
| |
| 10. | | WU, J.; KOBAYASHI, H.; STARK, S. C.; MENG, R.; GUAN, K.; TRAN, N. N.; GAO, S.; YANG, W.; RESTREPO-COUPE, N.; MIURA, T.; OLIVEIRA JUNIOR, R. C. de; ROGERS, A.; DYE, D. G.; NELSON, B. W.; SERBIN, S. P.; HUETE, A. R.; SALESKA, S. R. Biological processes dominate seasonality of remotely sensed canopy greenness in an Amazon evergreen forest. New Phytologist, v. 217, n. 4, p. 1507-1520, Mar. 2018.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Amazônia Oriental. |
|  |
| 11. | | WU, J.; GUAN, K.; HAYEK, M.; RESTREPO-COUPE, N.; WIEDEMANN, K. T.; XU, X.; WEHR, R.; CHRISTOFFERSEN, B. O.; MIAO, G.; SILVA, R. da; ARAUJO, A. C. de; OLIVEIRA JUNIOR, R. C. de; CAMARGO, P. B.; MONSON, R. K.; HUETE, A. R.; SALESKA, S. R. Partitioning controls on Amazon forest photosynthesis between environmental and biotic factors at hourly to interannual timescales. Global Change Biology, v. 23, n. 3, p. 1240-1257, Mar. 2017.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Amazônia Oriental. |
| |
| Registros recuperados : 11 | |
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
