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Biomedical subjects

R J Collier

Publications and source records attributed to R J Collier.

At least 145 records · Page 8Linked to original sources

Destripeptide insulin-like growth factor-I in milk from bovine somatotropin-treated cows.

Total somatomedins from milk of bovine somatotropin-treated cows were isolated and characterized to determine the relative amount of the three amino acid N-terminally truncated form of IGF-I (destripeptide IGF-I). The somatomedin fraction was isolated using organic solvent and solid-phase extractions followed by preparative reverse phase HPLC and affinity chromatography. The overall yield of IGF-I was 28%, and destripeptide IGF-I was recovered with similar efficiency. The isolated somatomedins were resolved by capillary zonal electrophoresis and identified using recombinant somatomedin standards. The concentration of destripeptide IGF-I relative to full length IGF-I was determined by amino terminal sequencing and by bioassay. Results from these experiments indicated that the level of destripeptide IGF-I in milk from somatotropin-treated cows was less than 3% of the IGF-I concentration. Destripeptide IGF-I is therefore a minor component of the somatomedins present in milk from treated cows and does not contribute significantly to the proliferative activity of this milk.

Animals↗

Serum half-life and in-vivo actions of recombinant bovine placental lactogen in the dairy cow.

The clearance rate of recombinant bovine placental lactogen (rbPL) from the blood serum of four lactating dairy cows was measured using a specific radioimmunoassay. Two animals were non-pregnant, while the other two were at approximately 120 days of gestation. The rbPL was administered as an i.v. bolus injection (4 mg total) via an indwelling jugular catheter. Blood samples were taken periodically for 180 min and assayed for rbPL. Analysis of the clearance curves for the bolus injection suggested a single-compartment model and a serum half-life of 7.25 min. In a second experiment with the same animals, following cessation of lactation, rbPL or bovine GH (bGH) were administered by s.c. injection (50 mg/day) for 5 consecutive days. Blood samples were taken twice per day during the treatment period and a 3-day pretreatment period. Samples were analysed for glucose, blood urea nitrogen (BUN), non-esterified fatty acids (NEFA), creatinine, insulin, insulin-like growth factor-I (IGF-I) and IGF-II, tri-iodothyronine (T3), progesterone and IGF-binding protein-2 (IGFBP-2) to determine whether rbPL mediates similar metabolic effects to those of bGH. Administration of bGH stimulated an increase in NEFA, glucose, T3 and insulin, whereas none of these variables was affected by rbPL. The plasma concentrations of IGF-I and IGF-II were both increased by treatment with rbPL but, to a lesser extent than occurred with bGH. Interestingly, BUN and IGFBP-2 concentrations were reduced equally by bGH and rbPL. These results suggest that rbPL does not necessarily act as a GH agonist but, rather, may have distinct effects on intermediary metabolism that could be mediated through another specific receptor.

Animals↗

Effect of growth hormone treatment on the distribution of insulin-like growth factor-I between plasma and lymph of lactating sheep.

Plasma and mammary efferent lymph concentrations of insulin-like growth factor I (IGF-I) were determined in lactating ewes before and after treatment with GH (10 mg/day) for 3 days. The lymph:plasma ratio of IGF-I increased from 0.34 to 0.47 after GH treatment when the IGF-I content of plasma increased by 19.4 nmol/l (from 32.1 nmol/l) and lymph by 13.7 nmol/l (from 10.7 nmol/l). This increase in the relative content of IGF-I in lymph was associated with increased lymph content of IGF-I in a lower molecular mass pool (nominally 50 kDa) derived by size exclusion chromatography. GH treatment increased the total binding capacity for IGF-I in both high (150 kDa) and low (50 kDa) molecular mass pools of plasma and the 150 kDa pool in lymph but there was a proportionally greater increase in 50 kDa total binding in lymph relative to plasma. Further, GH treatment increased the 'saturation' of the 50 kDa binding proteins but decreased the 'saturation' of the 150 kDa fraction, in both plasma and lymph. Ligand blot analysis of IGF-binding proteins (IGFBPs) in plasma and lymph showed that GH treatment of lactating sheep increased IGFBP-3 and decreased IGFBP-2 in plasma and lymph. Radioimmunoassay of IGFBP-2 showed that while GH treatment reduced the plasma content of IGFBP-2 by about half, the lymph:plasma ratio was increased from 0.68 to 0.87. GH treatment of lactating ewes not only increased the IGF-I content of plasma but increased the apparent efficiency of transfer of IGF-I across capillary endothelium to mammary efferent lymph.

Animals↗

Ruminant placental lactogens: structure and biology.

Ruminant placental lactogens (PL) are members of the somatotropin, prolactin gene family that are synthesized by trophectodermal binucleate cells. The structure and biology of PL has been studied in the cow, sheep, and goat. Ruminant PL have greater structural identity to prolactin than somatotropin, although they bind to both lactogenic and somatogenic receptors. The molecular weights of ovine and caprine PL are approximately 23,000, whereas bovine PL is larger (31,000 to 34,000) due to glycosylation. Placental lactogen is secreted into both the fetal and maternal circulations. The concentration of PL in the fetus decreases with advancing gestation, whereas PL concentration peaks in the maternal circulation during the last third of pregnancy then reaches a plateau. Furthermore, the maternal concentration of PL is 100- to 1,000-fold higher in sheep and goats than in cows. The precise factors that modulate secretion of PL are unknown, although placental mass and nutrition seem to play a role. Ruminant PL have both lactogenic and somatogenic biological activities and may also have unique activities mediated through a specific receptor. There is circumstantial evidence to suggest that PL plays a role in stimulating mammogenesis. Placental lactogen secreted into the fetal compartment may also help regulate fetal growth. Direct experimental data indicate that PL can regulate maternal intermediary metabolism. Thus, it may act as a partitioning agent to regulate nutrient supply for fetal growth. The precise biological function of PL in ruminants, therefore, still needs to be defined.

Amino Acid Sequence↗

Long-term effects of sometribove in lactating cows during a fourth consecutive lactation of treatment: insulin and somatotropin responses to glucose infusion.

The effect of sometribove (USAN, methionyl bST) on the endocrine pancreas and blood bST concentrations was investigated in 6 control and 6 treated Friesian cows, averaging 111 and 118 d postpartum in their fourth lactation of treatment. Each lactation the treated cows received sometribove injections (500 mg) every 2 wk (injection cycle) starting 60 +/- 3 d postpartum, increasing milk yield 3.3, 5.9, 1.9, and 4.2 kg/d in lactations 1, 2, 3, and 4, respectively. On d 8 of a fourth lactation injection cycle, blood was sampled for 390 min, starting 30 min before an intravenous glucose infusion (100 mg/kg) over a 20-min period. Preinfusion concentrations of glucose, insulin, and bST were elevated in sometribove-treated cows versus controls: 82.1 versus 74.4 mg/dl, 28.1 versus 19.7 microIU/ml, and 4.6 versus .9 ng/ml, respectively. Glucose infusion resulted in a rapid increase in blood glucose and insulin concentrations, followed by a sharp decline to preinfusion values across both treatments, resulting in similar net area under the curves for glucose and insulin. Blood bST concentrations remained unchanged. This study supports the concept that sometribove increases milk yield in dairy cows by chronically influencing homeorhetic mechanisms.

Animals↗

Stimulation of milk yield and feed intake by bovine placental lactogen in the dairy cow.

A 6 x 6 Latin square design was used to test the effects of recombinant bovine placental lactogen on milk yield, milk composition, feed intake, and blood hormone and metabolite levels in nonpregnant lactating cows. The six treatments (5, 10, 20, and 40 mg/d of placental lactogen, water as negative control, and 20 mg/d of bST as positive control) were administered by subcutaneous injection twice daily for 9 d. Blood samples were taken during the last 5 d of the treatment period. The three highest doses of placental lactogen increased milk yield, and there was a linear dose effect, although placental lactogen was less potent than bST. Milk concentrations of lactose, protein, and fat were not altered by any of the treatments. Dry matter intake was increased by two of the doses of placental lactogen, but not by bST. Blood urea N concentration was decreased in a dose-dependent manner by placental lactogen and was also decreased by bST. Similarly, serum insulin-like growth factor-I was increased in a dose-dependent manner by placental lactogen and was also increased by bST. Plasma concentrations of NEFA and glucose were increased by bST, but placental lactogen had little or no effect on either of these parameters. Thus, placental lactogen appears to act, in part, as a weak somatotropin agonist; however, it also appears to have specific activities, e.g., stimulating feed intake.

Animals↗

Effect of high doses of a sustained-release bovine somatotropin on antibody formation in dairy cows.

Eighty-two lactating Holstein cows received either one, three, or five concurrent, intramuscular injections of a unit dose (.6 g) of zinc methionyl bST (some-tribove) or five doses of the vehicle. Injections were administered at 14-d intervals from 60 d postpartum until the end of lactation or necropsy. Thirty-eight cows continued on the same treatment for a 2nd yr. Blood bST antibodies developed within the first 7 wk of treatment, and the number of cows with anti-bST binding generally declined with time. Thirteen out of 59 cows receiving bST developed binding activity > 25% (positives) during the 1st yr. At the .6-g dose level, no binding was detected after wk 15. Seven of the 13 positive cows were among the group randomly selected to continue on study during yr 2. In the 2nd yr, only 2 out of 24 bST-treated cows were positive. Binding activity was associated with the IgG fraction in serum. Binding capacities of antibodies ranged from .625 to 3.04 mg of bST/L, and affinities ranged from 1.14 x 10(8) to 3.14 x 10(8) L/mol. Cows considered to be clinically positive had performance similar to those of their herdmates having binding < 25%. No evidence of a pathologic effect of antibodies existed in treated cows, their calves, or fetuses. The presence of anti-bST antibodies did not affect milk production of the cow or growth of the calves conceived during bST treatment.

Animals↗

Nutrient balance and stage of lactation affect responses of insulin, insulin-like growth factors I and II, and insulin-like growth factor-binding protein 2 to somatotropin administration in dairy cows.

Six Holstein cows were used in a complete block design to examine effects of period of lactation and somatotropin (bST) administration on concentrations of insulin, insulin-like growth factors (IGF-I, IGF-II), and IGF-binding protein 2 (IGFBP-2). During late lactation, the dry period and the subsequent early lactation, cows received injections of NaHCO3 buffer for 5 d and bST for 7 d. Cows were in positive energy and protein balances during late lactation and the dry period and in slight negative balances during early lactation. Basal insulin concentrations were highest in late lactation (170 pmol/L), whereas bST concentrations were higher in early lactation (0.6 micrograms/L). Insulin was increased by bST in the dry period (255 pmol/L) and late lactation (149 pmol/L) but not in early lactation (14 pmol/L), probably because of greater availability of glucose during positive nutrient balance. Basal IGF-I was lowest in early lactation (63.6 micrograms/L) but was increased by bST during all periods. The IGF-I response to bST administration was lower during early lactation (74.1 micrograms/L) compared with late lactation (123.6 micrograms/L) and dry period (146.0 micrograms/L). The IGF-II concentrations were not affected by period of lactation of bST administration but IGF-II tended to be higher during bST administration when cows were dry. Concentration of IGFBP-2 was higher during early lactation when cows were in negative nutrient balance (479.5 micrograms/L) than during the dry period (289.2 micrograms/L) and was decreased with bST. These data support a role of insulin and IGF in regulation of milk production. Availability of nutrients may be involved in regulating these hormones, particularly during bST treatment.

Animal Nutritional Physiological Phenomena↗

Assessment of thermal status of somatotropin-injected lactating Holstein cows maintained under controlled-laboratory thermoneutral, hot and cold environments.

Two experiments, with a single-reversal design and 12 cows per experiment, were conducted to study the effects of somatotropin on thermal status of lactating cows under laboratory thermoneutral (18 to 22 degrees C, 30-50% relative humidity), hot (24-35 degrees C, 30-50% relative humidity) and cold (-5 (-) +5 degrees C, 50-55% relative humidity) conditions. Throughout the experiment six cows were injected with somatotropin (25 mg/d) and six with sodium bicarbonate. All injections were started the first day of the 30-d natural environmental period (22-35 degrees C and 41-97% relative humidity for summer experiment, and -5 (-) +5 degrees C and 4-25% relative humidity for winter experiment) before the cows were exposed alternatively to laboratory thermoneutral and hot or cold environments. The somatotropin-treated cows had higher energy intake (13 and 17%), heat production (19 and 25%), heat loss (36 and 24%) and milk energy (40 and 49%), than control cows under thermoneutral and hot conditions, respectively. The somatotropin-treated cows had higher heat production (18 and 10%), respiratory heat loss (27 and 17%) and milk energy (14 and 25%) than control cows under thermoneutral and cold conditions, respectively. The increased heat production associated with somatotropin was accompanied by increased heat losses. Part of the increased heat production was attributed to the increased milk energy and energy intake. These results suggest that increased heat production during somatotropin treatment was within the range that could be dissipated by the cows.

Animals↗

Anthrax toxin protective antigen: low-pH-induced hydrophobicity and channel formation in liposomes.

To probe the role of the protective antigen (PA) component of anthrax toxin in toxin entry into animals cells, we examined the membrane channel-forming properties and hydrophobicity of intact and trypsin-cleaved forms of the protein at various pH values. At neutral pH neither form caused release of entrapped K+ from unilamellar lipid vesicles. At pH values below 6.0, however, K+ was rapidly released upon addition of either the nicked PA (PAN) or the 63 kDa tryptic fragment of PA (PA63), which has been implicated in the toxin entry process. Under the same conditions intact PA exhibited only weak channel-forming activity, and PA20, the complementary tryptic fragment, showed no such activity. Both PA and PA63 exhibited enhanced hydrophobicity at acidic pH values, but the enhancement was greater and the pH threshold higher with PA63. Our findings indicate that proteolytic removal of PA20 from intact PA enables the residual protein, PA63, to adopt a conformation at mildly acidic pH values that permits it to insert readily and form channels in membranes. Thus acidic conditions within endocytic vesicles may trigger membrane insertion of PA63, which in turn promotes translocation of ligated effector moieties, edema factor or lethal factor, across the vesicle membrane into the cytosol.

Anthrax↗

Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells.

The interaction of protective antigen (PA), a component of the anthrax toxin, with receptors on the Chinese hamster ovary cell line CHO-K1 was characterized. Protective antigen binding at 4 degrees C is highly specific, concentration dependent, saturable (Kd = 0.9 nM), and reversible. Scatchard analysis indicates the presence of a single class of PA binding sites at a concentration of 10,000 +/- 2,000 per cell. Pretreatment of cells with a number of different proteases strongly inhibits PA binding, suggesting that the receptor may be at least partially proteinaceous. Direct chemical cross-linking of radioiodinated PA to the cell surface results in the appearance of a major band exhibiting an apparent molecular mass of 170 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The appearance of this band is completely inhibited by a 200-fold molar excess of unlabeled PA, indicating a high specificity for this interaction. Our results suggest that a cell surface protein(s) of 85 to 90 kDa is, or constitutes a portion of, a specific receptor for the PA.

Animals↗

The direct in vitro effect of insulin-like growth factors (IGFs) on normal bovine mammary cell proliferation and production of IGF binding proteins.

Mammary epithelial cells isolated from pregnant, nonlactating heifers were grown in vitro using collagen substrates. Using these systems, the truncated form of insulin growth factor-1 (IGF-1) (des-3-IGF-1), IGF-1, and IGF-2 all stimulated a significant (0.5 to 1 fold) increase in cell proliferation (des-3-IGF-1 greater than IGF-1 greater than IGF-2). When grown in media containing serum plus IGF-1, normal bovine mammary cells also produced and secreted at least four species of IGF-binding protein (IGFBP) ranging from 21K to 48K (as demonstrated by ligand blot analysis). However, cells grown in serum free media secreted detectable quantities of only 2 major forms of IGFBP of 34K and 48K. Using immunoblot analysis, these proteins were identified as IGFBP-2 and IGFBP-3, respectively. Both proteins were inducible by the addition of IGF to the serum free media (relative potency; IGF-1 greater than des-3-IGF-1 greater than IGF-2). Using RIA analysis, bovine mammary cells cultured in the presence of IGF-1 produced 20-25 ng/ml IGFBP-2 compared to control cultures which secrete approximately 1.0 ng/ml. Cells exposed to des-3-IGF-1 produced 40-60% less IGFBP-2 whereas insulin and IGF-2 did not stimulate significant IGFBP-2 production. These data indicate that normal bovine mammary cells secret IGFBP-2 and IGFBP-3. This secretion is stimulated by IGF-1 and des-3-IGF-1 suggesting a mechanism for regulating local IGF activity.

Animals↗

Stimulation of body weight gain of the mature female rat by bovine GH and bovine placental lactogen.

Mature female rats (200 g) were treated for 10 days with either recombinant bovine GH (bGH) or recombinant bovine placental lactogen (bPL) to compare the somatogenic responses elicited by these hormones. The treatments were administered by daily s.c. injection at four dose levels (0.19, 0.56, 1.67 and 5.0 mg/day). Both bGH and bPL stimulated significant increases in weight gain, but the slopes of the dose-response curves were different (P less than 0.05). Bovine PL was more potent than bGH (P less than 0.01) at the lowest dose, although there were no differences between treatment groups at the three higher doses. Feed consumption was stimulated more by bPL than bGH at all doses (P less than 0.001). The concentration of insulin-like growth factor-I (IGF-I) in blood plasma was increased by bGH in a dose-responsive manner and was higher than control at doses of 1.67 and 5 mg/day (P less than 0.05). Low doses of bPL stimulated increases in IGF-I similar to those with bGH. At the highest dose of bPL, however, there was no concomitant increase in plasma IGF-I. Nevertheless, the growth rate of the animals in this group matched that of the group given the highest dose of bGH. Receptor binding studies indicated that bPL bound to both GH and prolactin receptors. This is consistent with the growth data which suggests that bPL stimulated weight gain through a somatogenic mechanism as well as by another route, possibly mediated by lactogenic receptors.

Animal Nutritional Physiological Phenomena↗

Ontogeny of hepatic bovine growth hormone receptors in cattle.

A series of studies examined the binding characteristics and ontogeny of hepatic growth hormone binding sites in dairy bulls on d 2, 30, 180, and 365 of age. Binding of iodinated recombinant bovine growth hormone ([125I]rbGH) to liver membrane receptors was membrane protein-dependent. Receptors were considered growth hormone-specific, because physiological concentrations of bovine prolactin (bPRL) failed to displace [125I]rbGH from bovine hepatocyte membranes. Only 50% of [125I]rbGH was bound reversibly to hepatic microsomes. Addition of dithiothreitol (DTT) to the receptor-assay buffer increased the binding of [125I]rbGH to hepatic membranes in a time-dependent manner. Moderate concentrations of Ca++ and Mg++ in the receptor-assay buffer had no detectable effects on binding of [125I]rbGH to hepatic microsomes. In growing dairy bulls, specific binding of [125I]rbGH per milligram of membrane protein increased from 1.9 +/- 1.8% at d 2 to 14.1 +/- 1.8% at d 180 and then declined to 5.2 +/- 1.6% at d 365. Likewise, concentration of insulin-like growth factor (IGF)-I in serum was low during the 1st mo of age (d 2, 13.3 +/- 8.8 ng/ml; d 30, 9.7 +/- 8.8 ng/ml), but it became maximal at d 180 (151.0 +/- 8.8 ng/ml). Circulating concentrations of IGF-II increased linearly during the 1st yr of growth. Serum concentrations of GH, triiodothyronine, and thyroxine declined from 39.9 +/- 6.5, 2.7 +/- .2, and 75.4 +/- 4.6 ng/ml at d 2 to 16.5 +/- 6.5, 1.3 +/- .2, and 53.4 +/- 4.6 ng/ml at d 30, respectively, and remained low through 1 yr of age. Insulin concentration in serum did not change significantly with development. Results indicated that increasing concentrations of specific bGH receptors in the bovine liver may play a key role in regulating postnatal growth in cattle.

Aging↗

Effects of acute thermal stress and amount of feed intake on concentrations of somatotropin, insulin-like growth factor (IGF)-I and IGF-II, and thyroid hormones in plasma of lactating Holstein cows.

Our objective was to evaluate effects of acute thermal stress, independent of reduced feed intake caused by elevated temperatures, and of reduced feed intake in thermal comfort on plasma concentrations of somatotropin, insulin-like growth factors I and II, thyroxine, and triiodothyronine. Six Holstein cows (averaging 475 +/- 18 kg BW, 2.3 +/- .3 parities, and 96 +/- 12 d in lactation) surgically fitted with catheters in the hepatic portal vein, mesenteric vein, and intercostalis posterior artery were exposed to treatments of thermal comfort environments with ad libitum or restricted (75% of ad libitum) DM intake and a thermal stress environment with ad libitum intake in two balanced 3 x 3 Latin squares. Thermal stress increased rectal temperatures and respiration rates. Dry matter intake of the thermal-stressed cows offered feed ad libitum (11.1 +/- .7 kg/d) was similar to the experimentally imposed reduction in DM intake of the thermal comfort restricted group (11.5 +/- .7 kg/d). Dry matter intake of cows in thermal comfort was 15.1 +/- .7 kg/d. Plasma somatotropin concentrations tended (P less than .08) to decrease during thermal stress but were unchanged by amount of feed intake in thermal comfort environments. Concentrations of IGF-I were not affected by treatments. Concentrations of IGF-II tended (P less than .14) to increase with thermal stress compared with thermal comfort treatments. Thyroxine concentrations tended (P less than .15) to increase in the thermal stress treatment compared with the thermal comfort restricted intake treatment. Triiodothyronine tended (P less than .11) to decrease with restriction in feed intake in the thermal comfort environment.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Effects of somatotropin on milk yield and physiological responses during summer farm and hot laboratory conditions.

The effects of bST on performance and physiological responses of lactating cows was studied under farm summer and laboratory heat conditions. Twelve cows, 90 to 50 d postpartum, were injected with either bST or vehicle solution for 30 d under farm summer and 10 d under either laboratory thermoneutral or heat conditions. Somatotropin increased milk yield by 6.1 (21%), 8.1 (32%), and 7.3 kg (35%) under the farm summer, laboratory thermoneutral, and heat conditions, respectively. Somatotropin also increased milk fat by 15 and 19% and dry matter intake by 16 and 18% under laboratory thermoneutral and heat conditions, respectively. Somatotropin increased the efficiency of feed conversion into milk without any significant changes in body weight and temperatures. Somatotropin reduced plasma concentrations of triiodothyronine and cortisol and had no effect on plasma prolactin and insulin concentrations. Somatotropin did not increase water intake; however, hematocrit was decreased. The results suggest that stimulatory effects of bST on milk production are still observed on heat-stressed cows without any significant indications of additional heat stress.

Animals↗

Factors affecting insulin-like growth factor-I concentration in bovine milk.

To establish the naturally occurring range of insulin-like growth factor-I concentrations in bovine milk, samples from individual cows (n = 409) managed on five Missouri dairy herds were assayed. Parity, stage of lactation, and farm affected milk insulin-like growth factor-I concentration. Milk insulin-like growth factor-I concentration was higher in early lactation than mid and late lactation with concentrations in multiparous cows exceeding those in primiparous cows. Insulin-like growth factor-I concentration was negatively correlated to milk production the day of sample collection (r = -.15) and not correlated to predicted 305-d milk yields. Unprocessed bulk tank milk samples (n = 100) from a commercial processing plant had a mean concentration of insulin-like growth factor-I in milk of 4.32 ng/ml with a range of 1.27 to 8.10 ng/ml. This distribution was similar to the range detected in samples from individual cows, but values were lower than those reported for human milk. Concentration of insulin-like growth factor-I in milk was not altered by pasteurization (at 79 degrees C for 45 s). However, insulin-like growth factor-I was undetectable in milk heated to temperatures (121 degrees C for 5 min) required for infant formula preparation or in commercially available infant formula. These data indicated that insulin-like growth factor-I is a normal but quantitatively variable component of bovine milk that is not destroyed by pasteurization but is undetectable in infant formula. Concentration of insulin-like growth factor-I in bovine milk is lower than concentrations reported for human milk yet similar to those reported for human saliva.(ABSTRACT TRUNCATED AT 250 WORDS)

Analysis of Variance↗

Response of dairy cows to high doses of a sustained-release bovine somatotropin administered during two lactations. 1. Production response.

This study evaluated the effect of sometribove (zinc methionyl bST) in a sustained-release formulation administered to lactating cows at concentrations up to 3.0 g every 14 d over two lactations. Eighty-two lactating Holstein cows in their first, second, or third lactation were assigned to the study. Cows received .6, 1.8, or 3.0 g of bST in one, three, or five intramuscular injections of a unit dose (.6 g) every 2 wk. Controls received five injections of the vehicle (equivalent volume to the 3.0-g treatment) every 2 wk. Injections were administered from 60 +/- 3 d postpartum until dry-off or necropsy. Thirty-eight animals were continued on treatment for a second consecutive lactation. During the 1st yr of treatment, bST increased mean 3.5% FCM by 7.2, 9.4, and 8.4 kg/d over control production (21.1 kg/d). During the 2nd yr, milk response to .6, 1.8, and 3.0 g of bST averaged 10.6, 3.6, and 4.9 kg/d over controls (24.8 kg/d). The incidence of clinical mastitis increased in the 3.0-g group relative to controls during the 2nd yr. Thus, salable FCM averaged 8.1, 9.1, and 6.2 kg/d above controls (yr 1) and 12.1, 4.7, and -2.8 kg/d (yr 2) for the .6-, 1.8-, and 3.0-g groups. Salable FCM was unaffected by mastitis at a proposed commercial dose (.6 g). Milk fat, protein, lactose, calcium, phosphorus, zinc, magnesium, and ash concentrations were unaffected by bST treatment. Calculated energy, calcium, phosphorus, and protein balances also were unaffected except for early decreases of up to 5 Mcal/d, and 40, 20, and 600 g/d, respectively, until feed intake increased. Milk serum bST concentrations greater than the assay limit of sensitivity (1 ng/ml) were routinely measurable only at doses of 1.8 and 3.0 g. Results confirmed that bST concentrations in milk serum are exceedingly small. Overall, supraphysiological doses of sometribove increased milk production with little effect on composition. No toxic effects of bST were observed.

Animals↗