Colostrum Protein Research Articles

The effect of rivanol on the immune globulins of human colostrum

The behavior of immune globulins of colostrum was investigated during fractionation using rivanol and ethanol. It was found that, in contrast with serum immune globulins, a part of these proteins present in colostrum is precipitable with rivanol. It was also observed that the fraction of colostrum immune globulins which yields a heavy precipitation line in the cathode region of the immunoelectrophoreogram precipitated with normal antihuman serum, represents a heterogeneous mixture of proteins, from the point of view both of their electrophoretic mobility and of interaction with rivanol and solubility in dilute ethanol. We are dealing here with at least three types of protein molecules which all display identical antigen relationship to serum γ-and β2A-globulins. No differences were found between serum β2M-globulin and the colostrum protein of similar properties.

Whey Proteins of Drying-Off Secretions, Mastitic Milk, and Colostrum Separated by Ion-Exchange Cellulose

Summary Quarter milk samples from three cows in late lactation, dried off by intermittent milking, were analyzed for chlorides, pH, breed cell count, California Mastitis Test (CMT) score, and whey proteins. As milk production dropped, a rise in values for all constituents was observed. Increased whey protein was principally immune globulins resolved on DEAE-cellulose as four separate but probably nonhomogeneous components. The udder-formed proteins were secreted at a constant rate during the drying-off phase. Similar changes were observed in a case of induced mastitis. At 8 hr. a marked rise in blood serum albumin was found. The quarter then became nonfunctional. At 72 hr. the whey protein pattern was similar to the latter drying-off secretions. In both cases, the principal fraction was an immune-globulin that was not adsorbed on to the column. Though the relative concentrations of individual proteins of colostral whey were similar in magnitude to mastitic milk and latter drying-off secretions, the nonadsorbed immune globulin was markedly decreased and the bulk of the immune globulins appeared as a peak eluting with 0.05–0.075 M NaCl. A part of the difference was a colored component present in mastitic milk and drying-off secretions, but absent or in low concentration in colostrum. Euglobulin and pseudoglobulin prepared by two methods produced higher euglobulin/pseudoglobulin ratios from drying-off secretions than from colostrum. The amount of euglobulin and pseudoglobulin found and the elution pattern from DEAE-cellulose varied with the method and source. Thus, no peak could be described as principally a euglobulin or pseudoglobulin.

Ultracentrifuge and electrophoretic studies on the proteinuria of the new-born calf.

1. Many immunologically related components occur in bovine serum and colostrum, but certain components in each are absent in the other (specific components). Two components (or groups) occur in colostrum which do not appear in serum, and these can be associated with electrophoretically slow and fast colostrum components.2. Pre-colostral and adult urines contain low concentrations (<0·2 g./ 100 ml.) of protein which, though immunologically related to serum proteins, does not closely resemble any major serum component in physical properties.3. Urines collected during the period of proteinuria contain increased concentrations of protein (up to 2 g./ 100 ml.) which is immunologically related to both serum and colostrum. From the presence of material related to specific colostrum components (and the absence of specific serum components), the added protein evidently originates from colostrum rather than serum. The total added protein possesses components with electrophoretic mobilities covering a wide range, with appreciable protein faster than albumin at pH 8. From sedimentation studies, the added proteins resemble the slower sedimenting colostrum proteins (β-lactoglobulin and lactalbumin) and contain no observable material with the sedimentation behaviour of immune lactoglobulin.4. Immunologically, the added protein is related only to the electrophoretically faster of the specific colostrum components, and this applies also to post-colostral lymph in spite of its very high content of immune lactoglobulin. It follows that the specific electrophoretically slower colostrum components represent only a small proportion of the total immune lactoglobulin fraction.5. The presence in urine, collected during the period of proteinuria, of antibody activity (deriving originally from the calf's mother), and of protein with the approximate electrophoretic mobility of, but without the sedimentation behaviour of γ-globulin, is to be explained probably on the basis of molecular degradation at some stage between absorption from the intestine and excretion in the urine.6. The low molecular weight colostrum components, though present in low concentration in the lymph, are absent or below the detectable threshold in post-colostral sera (containing much material derived from immune lactoglobulin), and this is thought to be partly due to selective action by the kidney, allowing the passage of, and causing concentration of low molecular weight protein in the urine, whilst retaining higher molecular weight protein in the serum.7. The results show that the proteinuria of the new-born calf arose mainly from low molecular weight protein in the colostrum which was absorbed from the gut together with the immune lactoglobulin. Owing to the small molecular weight, this, the former protein, was subsequently cleared from the circulation probably by glomerular filtration, accounting for the difficulty of detecting them electrophoretically and ultracentrifugally. On the other hand, the immune lactoglobulin with its much higher molecular weight was not so cleared from the circulation and is readily detected there.The authors wish to thank Sir Alan Drury, F.R.S., for his support during the course of this work, Mr N. Buttress and Mr D. Hardman for technical assistance and Mr J. Clark for assistance in the care and handling of the calves.

C-reactive protein in human colostrum.

SummaryC‐reactive protein (CRP) was determined in colostrum and milk samples from 12 mothers with positive reactions in their sera. CRP could not be demonstrated in any of 63 colostrum or milk specimens, and a transfer of CRP from mother to child by ingestion of colostrum or milk thus is unlikely. This supports the opinion that the infant is capable of producing CRP in early life.

初乳蛋白に関する研究

初乳ホエーを硫酸ソーダと硫安で塩析したが前者に於て濃度15%前後よりカゼイン以外の比較的易動度の早い蛋白が落ち,18.23%前後をピークとして上記のものより易動度の遅い蛋白が落ちている。硫安の場合1/2.5∼1/2.25飽和で多量の蛋白が落ち,飽和度1/3∼1/2.5では比較的易動度の遅い蛋白が落ちている。そして,之等の蛋白は,多少性質が異なつている様であるが更に微細な塩析と酸側アルカリ側で泳動する事等により泳動的に明確に単一蛋白である事を証明してその差異を究明したいと思う。蛋白の沈澱の際の燐の結合状態は複雑であり乳蛋白の放射能比が高く初乳の蛋白が高い事より燐代謝の旺な事を示している。又ホエー蛋白の放射能比がカゼインより大なる事は乳汁蛋白の合成機構及び乳汁中の灰分の結合状態の複雑性を示嗟して居り,今後の研究に待ちたい。終りにのぞみ終始御懇篤なる御指導を賜わつた恩師前野正久教授に篤く謝意を表す。

Electrophoretic Observation on Proteins of Prepartum Milk, Colostrum and Calf's Blood Serum

Influence of parturition upon the constituents of Saanen goat's and Holstein cow's milk was investigated in relation to the stage of prepartum and postpartum.The results obtained here are briefly summarised as follows:-The prepartum milk was almost resemble to colostrum in general. But in the case of goats it contained more milk-solids, protein and little less lactose than their colostrum. In the case of cow, however, prepartum milk contained less milk-solids, fat, and protein as compared with her colostrum. This difference between the dairy goats and cows may be due to the species specific lactating process.Electrophoretic analysis demonstrated that the prepartum milk and colostrum of these two kinds of dairy animals contained much immune lactoglobulin as compared with their aged milk. In cow's milk the immune component rose from the seventh day before parturition toward the colostrum period, but in goats milk it declined from the third day before parturition toward the colostrum period, and falling rapidly two days after parturition. This component was almost precipitated with (NH4)2SO4 at 0.4 saturation.Casein in prepartum milk or colostrum, especially in the former, was hardly precipitated with acid, but such remaining casein type protein was able to be precipitated entirely with rennet at pH 5.4.

Electrophoretic Observation on Proteins of Prepartum Milk, Colostrum and Calf's Blood Serum

Electrophoretic observation was carried out on blood sera of three calves. Sera of new born calves contained no γ-globulin. It appeared after ingestion of colostrum, but its content was very low for two Holstein calves, it may be, as their initial suckling of colostrum was too late after birth (one day after birth). The serum of another calf (Guernsey) which received colostrum within 10 hours after birth contained it considerably.This globulin which appeared in the serum of calf during ingestion period of colostrum fairly agreed with colostrum globulin electrophoretically. The slowest moving component, which is present in cow's serum, was apparently appreciable in the serum of calf after three months of birth, but it was still less than that of cow's serum. This component is probably no related to ingestion of colostrum.Als in new born goat's serum, no γ-globulin was found. But appearance of this component was not successfully found within several hours after initial suckling.

初乳蛋白に關する研究

Studies on proteins of colostrum were planed to research their characters, and following, results were obtained by the first experiments.1 Buffer action of colostrum was very great and quantities of free calciums in ultra-filtrate were comparatively small.2 By electrophoretic patterns colostrum contained about five or six different proteins and were possible to be fractionated with salts.3 Ultra-filtrate of colostrmn contained above four proteins and it's electrophoretic patterns were like to serums'.

初乳蛋白に関する研究

初乳蛋白に関する研究

Electrophoretic Properties of Milk Proteins. II. Effect of Heating to 300° F. by Means of the Mallory Small-tube Heat Exchanger on Skimmilk Proteins

Mellander (12) was the first to obtain an electrophoretic pattern of skimmilk and of casein. Other investigators (4, 5, 6, 7, 8, 14, 21) studied various preparations of casein. Slatter and Van Winkle (15) heated skimmilk to 65, 75 and 85 ° C. for 30 rain. and observed changes in the electrophoretic patterns as a result of the heat treatment. The whey proteins of milk and colostrum have received considerable attention in the past few years (1, 2, 3, 7, 9, 11, 16, 17, 18, 19). While whey is considered to contain six or more components, only the immune globulins (16, 17) and fl-lactoglobulin (1, 2, 9, 11, 18, 19) have been studied in detail. The present research was undertaken to compare the electrophoretic properties of raw skimmilk with those of the same skimmilk heated at one well controlled heating temperature and time of exposure.

Route of absorption of colostrum globulin in the newborn animal.

THE feeding of colostrum to the newborn of many species is followed by the appearance of certain of the colostrum proteins in the blood serum1–3. This capacity to absorb large amounts of unchanged protein disappears within 24–48 hr. of birth2. In ruminants, the proteins, which are associated with the antibodies of the colostrum, have been identified by salt fractionation as euglobulin and pseudo-globulin I4. Their behaviour on electrophoresis is similar to that of the γ-globulin of adult serum5.

Properties of the Colostrum of the Dairy Cow. II. Effect of Prepartal Rations upon the Nitrogenous Constituents

Summary Twenty pregnant heifers and cows were paired according to breed and to number and stage of gestation. For 7 weeks (average) before parturition, one group received a high-protein ration and the other a low-protein ration. The rations did not effect a significant difference in the levels of total protein, of casein, and of albumin-globulin fractions of colostrum and early milk from the foregoing groups. Non-protein nitrogen levels were higher in colostrum and early milk from cows of the high-protein group, but the differences were significant only in samples after the first three collections postpartum. The decrease in concentrations of the protein fractions of mammary secretions during the transition period tended to follow a logarithmic curve for the first four to six milkings, after which the rate of decline was less rapid. Changes in non-protein nitrogen seemed to continue at approximately the same logarithmic rate in samples representing the second through the sixteenth milkings. Rates of change of the nitrogenous constituents were similar in colostrum and in milk from cows receiving either the high- or the low-protein rations. Analysis of intra-group data indicated that colostrum from first-lactation cows receiving the high-protein ration contained higher levels of albumin-globulin nitrogen than did second-lactation cows receiving the same ration. Only small differences were observed after the first four milkings. Similar differences between heifers and cows fed the low-protein ration were not evident; the values for both of these lactation groups were between those of the heifers and cows receiving the high-protein ration. Deviations from the mean of values for nitrogen fractions for individual cows within the various groups were considerably greater during the early colostral period than later, as the composition of milk approached normal. Total protein and albumin-globulin contents of early colostrum were related to degree of mammary edema only to the extent that the averages of each of these protein fractions were higher from the ten cows judged to have the more severe edema than from the ten cows with the less severe edema. The rate of decline of total protein and of albumin-globulin contents of mammary secretions during the transition period was not related to the degree of mammary edema.

The Proteins of Cow's Colostrum. Part I. The Relation between the Euglobulin and Pseudoglobulin of Cow's Colostrum

The Proteins of Cow's Colostrum. Part I. The Relation between the Euglobulin and Pseudoglobulin of Cow's Colostrum