Characterizing the Protein Profile of Bovine Colostrum and Transition Milk
Conference Year
January 2019
Abstract
Colostrum plays a vital role in the nutrition, development, and immunity of a newborn calf. In colostrum, immunoglobulin G (IgG) is one example of a bioactive low abundance protein that is widely known. Many other proteins besides IgG are suspected to affect the quality of colostrum in terms of systemic benefit to the calf and provide insight into the mammary health and function of the dam. This study aimed to characterize the protein profile of colostrum, and changes in this proteome across parity and days post-parturition. Colostrum and transition milk samples were collected at milkings 1, 2, 4, and 14 (M1, M2, M3, and M14, respectively) after calving from multiparous and primiparous cows. Samples were fractionated and enriched prior to analysis for low abundance proteins in the skimmed milk by liquid chromatography - tandem mass spectroscopy (LC-MS/MS). Identified proteins were analyzed using a mixed procedure in SAS to identify effects of parity (P), milking number (MN), and their interaction (MNxP). A total of 86 proteins were identified by LC-MS/MS, of which 3 were affected by P, 78 were affected by MN, and 36 were affected by MNxP. Prominent ontological groupings within proteins affected by MN included defense/immunity proteins, such as immunoglobulins. Proteins involved in the plasminogen activating cascade and more broadly, blood coagulation, were affected by MNxP. The results of this study add to increasing knowledge of the colostrum and transition milk proteomes and is the first to find evidence of different abundances of these proteins when examined across P, MN, and MNxP. These findings aid in the identification of potential milk protein biomarkers for mammary health during the early post partum period.
Primary Faculty Mentor Name
Dr. Sabrina Greenwood
Status
Undergraduate
Student College
College of Agriculture and Life Sciences
Program/Major
Animal Science
Primary Research Category
Biological Sciences
Characterizing the Protein Profile of Bovine Colostrum and Transition Milk
Colostrum plays a vital role in the nutrition, development, and immunity of a newborn calf. In colostrum, immunoglobulin G (IgG) is one example of a bioactive low abundance protein that is widely known. Many other proteins besides IgG are suspected to affect the quality of colostrum in terms of systemic benefit to the calf and provide insight into the mammary health and function of the dam. This study aimed to characterize the protein profile of colostrum, and changes in this proteome across parity and days post-parturition. Colostrum and transition milk samples were collected at milkings 1, 2, 4, and 14 (M1, M2, M3, and M14, respectively) after calving from multiparous and primiparous cows. Samples were fractionated and enriched prior to analysis for low abundance proteins in the skimmed milk by liquid chromatography - tandem mass spectroscopy (LC-MS/MS). Identified proteins were analyzed using a mixed procedure in SAS to identify effects of parity (P), milking number (MN), and their interaction (MNxP). A total of 86 proteins were identified by LC-MS/MS, of which 3 were affected by P, 78 were affected by MN, and 36 were affected by MNxP. Prominent ontological groupings within proteins affected by MN included defense/immunity proteins, such as immunoglobulins. Proteins involved in the plasminogen activating cascade and more broadly, blood coagulation, were affected by MNxP. The results of this study add to increasing knowledge of the colostrum and transition milk proteomes and is the first to find evidence of different abundances of these proteins when examined across P, MN, and MNxP. These findings aid in the identification of potential milk protein biomarkers for mammary health during the early post partum period.