{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/19207"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/19207","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Chemical and physical properties of bovine alpha-lactalbumin, beta-casein and genetically altered bovine beta-casein produced in the milk of transgenic mice","abstract":"The genomic bovine $\\alpha$-lactalbumin gene (1.7 kb) and the bovine $\\beta$-casein gene (8.5 kb) linked to bovine $\\alpha$-lactalbumin 5$\\prime$ flanking region (2.0 kb) were expressed in two lines of transgenic mice, $\\alpha$-114 and $\\alpha\\beta$ 34, respectively. Whey proteins, caseins, or skim milk proteins of the transgenic mouse milk containing bovine $\\alpha$-lactalbumin or bovine $\\beta$-casein were analyzed and separated by polyacrylamide gel electrophoresis (PAGE), using SDS, urea, or native (non-denaturing) conditions. Using PAGE followed by immunoblotting, both heterologous proteins were proved as identical as the native proteins in the molecular weight and the charge. The estimated expression level of bovine $\\alpha$-lactalbumin and $\\beta$-casein was about 1.0 mg/ml and 3.0 mg/ml, respectively. The expression level of bovine $\\alpha$-lactalbumin was lactation-dependent, which was higher in early lactation than that in late lactation stage. Calcium binding of the heterologous bovine $\\alpha$-lactalbumin was also the same as native bovine $\\alpha$-lactalbumin. The phosphorylation level of the bovine $\\beta$-casein expressed in the transgenic mouse milk was identical to the native bovine $\\beta$-casein. The glycosylated bovine $\\alpha$-lactalbumin and the N-terminal amino acid sequence of purified bovine $\\alpha$-lactalbumin were characterized and determined. The physical properties of transgenic mouse milks were changed due to the heterologous expression of the bovine $\\beta$-casein or $\\alpha$-lactalbumin in the mouse milks. An increased moisture of transgenic mouse milk containing bovine $\\alpha$-lactalbumin was observed. However, the milk composition of transgenic mouse milk containing bovine $\\beta$-casein did not change significantly. In addition, two chymosin-resistant and one plasmin-resistant bovine $\\beta$-casein genomic constructs were generated and microinjected to generate transgenic mice. Mouse milk containing each of the three mutant $\\beta$-caseins was produced and analyzed by immunoblotting with a bovine $\\beta$-casein specific antibody. The mice carrying one of the chymosin-resistant gene constructs produced the milk containing mutant bovine $\\beta$-casein with the expected molecular weight. The result of rennin digestion demonstrated that the peptide bond of 192-193 in the mutant protein was chymosin-resistant. However, the mice carrying the plasmin-resistant $\\beta$-casein produced two proteins in their milk which reacted with bovine $\\beta$-casein antibody and had smaller molecular weights than that of the expected mutant $\\beta$-casein.","abstract_html":"The genomic bovine α-lactalbumin gene (1.7 kb) and the bovine β-casein gene (8.5 kb) linked to bovine α-lactalbumin 5$\\prime$ flanking region (2.0 kb) were expressed in two lines of transgenic mice, α-114 and αβ 34, respectively. Whey proteins, caseins, or skim milk proteins of the transgenic mouse milk containing bovine α-lactalbumin or bovine β-casein were analyzed and separated by polyacrylamide gel electrophoresis (PAGE), using SDS, urea, or native (non-denaturing) conditions. Using PAGE followed by immunoblotting, both heterologous proteins were proved as identical as the native proteins in the molecular weight and the charge. The estimated expression level of bovine α-lactalbumin and β-casein was about 1.0 mg/ml and 3.0 mg/ml, respectively. The expression level of bovine α-lactalbumin was lactation-dependent, which was higher in early lactation than that in late lactation stage. Calcium binding of the heterologous bovine α-lactalbumin was also the same as native bovine α-lactalbumin. The phosphorylation level of the bovine β-casein expressed in the transgenic mouse milk was identical to the native bovine β-casein. The glycosylated bovine α-lactalbumin and the N-terminal amino acid sequence of purified bovine α-lactalbumin were characterized and determined. The physical properties of transgenic mouse milks were changed due to the heterologous expression of the bovine β-casein or α-lactalbumin in the mouse milks. An increased moisture of transgenic mouse milk containing bovine α-lactalbumin was observed. However, the milk composition of transgenic mouse milk containing bovine β-casein did not change significantly. In addition, two chymosin-resistant and one plasmin-resistant bovine β-casein genomic constructs were generated and microinjected to generate transgenic mice. Mouse milk containing each of the three mutant β-caseins was produced and analyzed by immunoblotting with a bovine β-casein specific antibody. The mice carrying one of the chymosin-resistant gene constructs produced the milk containing mutant bovine β-casein with the expected molecular weight. The result of rennin digestion demonstrated that the peptide bond of 192-193 in the mutant protein was chymosin-resistant. However, the mice carrying the plasmin-resistant β-casein produced two proteins in their milk which reacted with bovine β-casein antibody and had smaller molecular weights than that of the expected mutant β-casein.","abstract_has_math":true,"creators":["Jeng, Shin-Yi"],"institution":"University of Illinois at Urbana-Champaign","degree_name":"Ph.D.","degree_level":"Dissertation","degree_discipline":"Food Science and Human Nutrition","degree_department":null,"school":null,"contributors":["Jimenez-Flores, Rafael"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2011,"date_issued":"2011-05-07T12:00:11Z","date_published":"2011-05-07T12:00:11Z","updated_at":"2026-07-22T22:25:12Z","subjects":["Agriculture, Food Science and Technology","Biology, Molecular"],"languages":["eng"],"rights":["Copyright 1996 Jeng, Shin-Yi"],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["9780591087307","AAI9702549","(UMI)AAI9702549"],"render_values":[{"text":"9780591087307","href":null,"code":true},{"text":"AAI9702549","href":null,"code":true},{"text":"(UMI)AAI9702549","href":null,"code":true}]}]},"links":{"outbound_url":"http://hdl.handle.net/2142/19207","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Jimenez-Flores, Rafael"]},{"key":"dc:creator","label":"Author","values":["Jeng, Shin-Yi"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2011-05-07T12:00:11Z","10000-01-01","1996"]},{"key":"dc:type","label":"Dc Type","values":["text"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Food Science and Human Nutrition"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Ph.D."]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["University of Illinois at Urbana-Champaign"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Agriculture, Food Science and Technology","Biology, Molecular"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Copyright 1996 Jeng, Shin-Yi"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["9780591087307","AAI9702549","(UMI)AAI9702549","http://hdl.handle.net/2142/19207"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["The genomic bovine $\\alpha$-lactalbumin gene (1.7 kb) and the bovine $\\beta$-casein gene (8.5 kb) linked to bovine $\\alpha$-lactalbumin 5$\\prime$ flanking region (2.0 kb) were expressed in two lines of transgenic mice, $\\alpha$-114 and $\\alpha\\beta$ 34, respectively. Whey proteins, caseins, or skim milk proteins of the transgenic mouse milk containing bovine $\\alpha$-lactalbumin or bovine $\\beta$-casein were analyzed and separated by polyacrylamide gel electrophoresis (PAGE), using SDS, urea, or native (non-denaturing) conditions. Using PAGE followed by immunoblotting, both heterologous proteins were proved as identical as the native proteins in the molecular weight and the charge. The estimated expression level of bovine $\\alpha$-lactalbumin and $\\beta$-casein was about 1.0 mg/ml and 3.0 mg/ml, respectively. The expression level of bovine $\\alpha$-lactalbumin was lactation-dependent, which was higher in early lactation than that in late lactation stage. Calcium binding of the heterologous bovine $\\alpha$-lactalbumin was also the same as native bovine $\\alpha$-lactalbumin. The phosphorylation level of the bovine $\\beta$-casein expressed in the transgenic mouse milk was identical to the native bovine $\\beta$-casein. The glycosylated bovine $\\alpha$-lactalbumin and the N-terminal amino acid sequence of purified bovine $\\alpha$-lactalbumin were characterized and determined. The physical properties of transgenic mouse milks were changed due to the heterologous expression of the bovine $\\beta$-casein or $\\alpha$-lactalbumin in the mouse milks. An increased moisture of transgenic mouse milk containing bovine $\\alpha$-lactalbumin was observed. However, the milk composition of transgenic mouse milk containing bovine $\\beta$-casein did not change significantly. In addition, two chymosin-resistant and one plasmin-resistant bovine $\\beta$-casein genomic constructs were generated and microinjected to generate transgenic mice. Mouse milk containing each of the three mutant $\\beta$-caseins was produced and analyzed by immunoblotting with a bovine $\\beta$-casein specific antibody. The mice carrying one of the chymosin-resistant gene constructs produced the milk containing mutant bovine $\\beta$-casein with the expected molecular weight. The result of rennin digestion demonstrated that the peptide bond of 192-193 in the mutant protein was chymosin-resistant. However, the mice carrying the plasmin-resistant $\\beta$-casein produced two proteins in their milk which reacted with bovine $\\beta$-casein antibody and had smaller molecular weights than that of the expected mutant $\\beta$-casein.","Made available in DSpace on 2011-05-07T12:00:11Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9702549.pdf: 11911303 bytes, checksum: 6d3f5d6b32e20b174fd03507ee141cf9 (MD5) Previous issue date: 1996","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:35:22Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:13:55-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"]},{"key":"dc:title","label":"Title","values":["Chemical and physical properties of bovine alpha-lactalbumin, beta-casein and genetically altered bovine beta-casein produced in the milk of transgenic mice"]}]}],"canonical_facts":{"dc:contributor":["Jimenez-Flores, Rafael"],"dc:creator":["Jeng, Shin-Yi"],"dc:date":["2011-05-07T12:00:11Z","10000-01-01","1996"],"dc:description":["The genomic bovine $\\alpha$-lactalbumin gene (1.7 kb) and the bovine $\\beta$-casein gene (8.5 kb) linked to bovine $\\alpha$-lactalbumin 5$\\prime$ flanking region (2.0 kb) were expressed in two lines of transgenic mice, $\\alpha$-114 and $\\alpha\\beta$ 34, respectively. Whey proteins, caseins, or skim milk proteins of the transgenic mouse milk containing bovine $\\alpha$-lactalbumin or bovine $\\beta$-casein were analyzed and separated by polyacrylamide gel electrophoresis (PAGE), using SDS, urea, or native (non-denaturing) conditions. Using PAGE followed by immunoblotting, both heterologous proteins were proved as identical as the native proteins in the molecular weight and the charge. The estimated expression level of bovine $\\alpha$-lactalbumin and $\\beta$-casein was about 1.0 mg/ml and 3.0 mg/ml, respectively. The expression level of bovine $\\alpha$-lactalbumin was lactation-dependent, which was higher in early lactation than that in late lactation stage. Calcium binding of the heterologous bovine $\\alpha$-lactalbumin was also the same as native bovine $\\alpha$-lactalbumin. The phosphorylation level of the bovine $\\beta$-casein expressed in the transgenic mouse milk was identical to the native bovine $\\beta$-casein. The glycosylated bovine $\\alpha$-lactalbumin and the N-terminal amino acid sequence of purified bovine $\\alpha$-lactalbumin were characterized and determined. The physical properties of transgenic mouse milks were changed due to the heterologous expression of the bovine $\\beta$-casein or $\\alpha$-lactalbumin in the mouse milks. An increased moisture of transgenic mouse milk containing bovine $\\alpha$-lactalbumin was observed. However, the milk composition of transgenic mouse milk containing bovine $\\beta$-casein did not change significantly. In addition, two chymosin-resistant and one plasmin-resistant bovine $\\beta$-casein genomic constructs were generated and microinjected to generate transgenic mice. Mouse milk containing each of the three mutant $\\beta$-caseins was produced and analyzed by immunoblotting with a bovine $\\beta$-casein specific antibody. The mice carrying one of the chymosin-resistant gene constructs produced the milk containing mutant bovine $\\beta$-casein with the expected molecular weight. The result of rennin digestion demonstrated that the peptide bond of 192-193 in the mutant protein was chymosin-resistant. However, the mice carrying the plasmin-resistant $\\beta$-casein produced two proteins in their milk which reacted with bovine $\\beta$-casein antibody and had smaller molecular weights than that of the expected mutant $\\beta$-casein.","Made available in DSpace on 2011-05-07T12:00:11Z (GMT). No. of bitstreams: 2 license.txt: 4922 bytes, checksum: 910b249b4beec47e7ab768910c8f966f (MD5) 9702549.pdf: 11911303 bytes, checksum: 6d3f5d6b32e20b174fd03507ee141cf9 (MD5) Previous issue date: 1996","Item marked as restricted to the 'UIUC Users [automated]' Group (id=2) by Howard Ding (hding2@illinois.edu) on 2011-05-07T14:35:22Z Item is restricted indefinitely.","Restriction data tranferred 2014-07-01T11:13:55-05:00 Original Data Group with Access UIUC Users [automated] Release Date: none Reason: ETDs are only available to UIUC Users without author permission","ETDs are only available to UIUC Users without author permission","U of I Only"],"dc:identifier":["9780591087307","AAI9702549","(UMI)AAI9702549","http://hdl.handle.net/2142/19207"],"dc:language":["eng"],"dc:rights":["Copyright 1996 Jeng, Shin-Yi"],"dc:subject":["Agriculture, Food Science and Technology","Biology, Molecular"],"dc:title":["Chemical and physical properties of bovine alpha-lactalbumin, beta-casein and genetically altered bovine beta-casein produced in the milk of transgenic mice"],"dc:type":["text"],"thesis:degree_discipline":["Food Science and Human Nutrition"],"thesis:degree_level":["Dissertation"],"thesis:degree_name":["Ph.D."],"thesis:institution_name":["University of Illinois at Urbana-Champaign"]},"updated_at":"2026-07-22T22:25:12Z"}