The Distribution of Extracorpuscular Hemoglobin in Circulating Plasma*†

Lathem, Willoughby; Worley, William E.

doi:10.1172/jci103823

Cited by 79 publications

(35 citation statements)

References 9 publications

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“…The significance of this large difference in maximal rates of hemoglobin catabolism is not clear at the present time. From reported measurements in man of the rate of hemoglobin-haptoglobin catabolism (25) and our previous measurements of rates of NEM-treated erythrocyte catabolism (4) this phenomenon also exists in man.…”

Section: Introductionmentioning

confidence: 53%

The Production of Carbon Monoxide from Hemoglobin In Vivo*

Coburn¹,

Williams²,

White³

et al. 1967

J. Clin. Invest.

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Summary. Dogs anesthetized with pentobarbital were shown to produce carbon monoxide at an average rate of 0.21 + (SD) 0.05 ml per hour. After intravenous injection of erythrocytes damaged by incubation with N-ethylmaleimide, CO was produced in excess of base-line production for 3 to 4 hours with an average yield of 0.89 + (SE) 0.046 umole of carbon monoxide to 1 Mmole of heme degraded.After intravenous injection of N-ethylmaleimide (NEM)-treated erythrocytes containing hemoglobin labeled with 14carbon, 14CO was produced. Its specific activity was approximately one-eighth that of the injected heme. It was also produced after intravenous injection of solutions of hemoglobin-14C and of reconstituted methemoglobin containing hemin-14C, but not after injections of methemoglobin containing globin-14C. The average yields of 14CO from metabolized heme in the experiments with damaged erythrocytes and hemoglobin solutions were 89 + (SE) 4.6 and 97 + (SE) 17.0%, respectively. These results demonstrate that the CO produced during hemoglobin degradation arises from the heme moiety.The yield of 14CO after injection of hemoglobin-14C solutions decreased significantly to values of 35 and 42% in two experiments when exogenous CO was added to the body stores, resulting in blood carboxyhemoglobin levels of 11.3 and 13.2% saturation. This finding suggests that oxidative metabolism is required during catabolism of hemoglobin to CO and that carboxyhemoglobin levels in this range are sufficient to cause inhibition.After intravenous injection of either hemin-14C or protoporphyrin-14C, 14CO was also produced. After injection of protoporphyrin-14C labeled bilirubin was isolated from gall bladder bile, and labeled hemin was isolated from the liver. It is thus very likely that protoporphyrin is converted to heme before the formation of CO.There was a large difference between the maximal rates of catabolism of hemoglobin to CO observed after injection of damaged erythrocytes and hemoglobin solutions. The limiting parameters in these processes are not yet clear.

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Section: Introductionmentioning

confidence: 53%

The Production of Carbon Monoxide from Hemoglobin In Vivo*

Coburn¹,

Williams²,

White³

et al. 1967

J. Clin. Invest.

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“…A catheter was placed in the urinary bladder and an indwelling needle was inserted in the brachial artery. Arterial blood was withdrawn and hemolyzed according to methods previously described (6), and priming and sustaining infusions of hemoglobin were prepared. The priming infusions contained approximately 2.0 Gm.…”

Section: Methodsmentioning

confidence: 99%

“…The demonstration (2,3) that plasma proteins possess the property of binding hemoglobin and that hemoglobin may circulate in both the free and unbound states (4)(5)(6) has invalidated the conceptual basis of these studies. Consequently many of the previous concepts of renal hemoglobin transport are no longer tenable and must be revised.…”

mentioning

confidence: 99%

“…Observations of hemoglobin binding in vivo and in vitro have established that the capacity of plasma proteins to bind hemoglobin is limited (3)(4)(5)(6). Since this capacity is near the plasma level at which hemoglobinuria characteristically occurs, it has been suggested (4,5) that the limitation imposed on hemoglobin excretion at low plasma levels is related to protein-binding and that only when the binding capacity is exceeded and hemoglobin circulates in the free, unbound state does hemoglobinuria occur.…”

mentioning

confidence: 99%

“…The total hemoglobin content of plasma and urine was determined by the method of Evelyn and Malloy (8). The concentrations of free hemoglobin, protein-bound hemoglobin and methemalbumin in plasma and urine were determined by a paper electrophoretic method previously described (6). This method consisted of the separation of these moieties on paper after overnight electrophoresis utilizing a phosphate buffer, pH 7.0, ionic strength 0.05.…”

mentioning

confidence: 99%

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The Renal Excretion of Hemoglobin: Regulatory Mechanisms and the Differential Excretion of Free and Protein-Bound Hemoglobin*†

Lathem¹

1959

J. Clin. Invest.

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Plasma Hemoglobin Concentration in Umbilical Cord Blood

ANDERSON¹

1963

Arch Pediatr Adolesc Med

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The concentration of hemoglobin in the plasma of normal human subjects has recently been reexamined in our laboratory, employing modified methods for blood sampling and for hemoglobin measurement.1,2 Study of 25 ambulatory adults revealed a mean value for plasma hemoglobin concentration (PHgbC) of 0.31 mg. per 100 ml., with a range of 0.16 to 0.58 mg. per 100 ml.As part of a broad study of PHgbC in normal subjects, preliminary observations were made on blood samples obtained from 6 women at the time of parturition and from the placental segment of the umbilical vein immediately after separation of the newborn infants. Although PHgbC was within the normal range for the 6 maternal samples, all of the umbilical vein samples yielded elevated values, half of them in the range 10 to 20 times the mean value for normal adults. Since to our knowledge this phenomenon had not been previously described, a detailed investigation was undertaken: (a) in order to confirm the preliminary findings and (b) to attempt to correlate the elevated values in umbilical vein samples with the infants' hématologie status at birth and any pertinent features of the pregnancy, labor, and delivery.The present report summarizes clinical, hématologie, and blood chemical studies on 30 normal infants and their mothers. Materials and MethodsThe subjects were private or ward patients con¬ fined at the St. Louis Maternity Hospital, affiliated with the Barnes Hospital Group. Two-thirds of the patients were white ; one-third were Negro.Collection of Blood Samples.-The technique of blood collection has been detailed in a previous publication.1Umbilical Vein Blood.-Sterile equipment was employed, and the investigators followed the routine scrub, gown, mask, and glove procedures recom¬ mended for the attending obstetricians. As soon as the infant had been delivered, 2 clamps were placed across the cord within 12 in. of the umbilicus, and the cord was cut between the clamps. A 15-gauge needle attached to a 14 in. length of polyvinyl tubing was immediately inserted cleanly into the umbilical vein on the placental segment of cord projecting from the introitus. The first 5 ml. of blood to flow by gravity was collected in a heparinized tube to be used for subsequent determination of hemoglobin, hematocrit, differential nucleated cell count, ABO blood group, Rh type, and direct Coombs test. Eight to 10 ml. was then collected with great care in each of 2 siliconized centrifuge tubes whose inner walls were coated with a fine mist of heparin solution. The tubes were promptly capped and centrifuged, and the supernatant plasma was separated and recentri fuged, as previously described.1 The plasma was used for determination of plasma hemoglobin

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The Distribution of Extracorpuscular Hemoglobin in Circulating Plasma*†

Cited by 79 publications

References 9 publications

The Production of Carbon Monoxide from Hemoglobin In Vivo*

The Production of Carbon Monoxide from Hemoglobin In Vivo*

The Renal Excretion of Hemoglobin: Regulatory Mechanisms and the Differential Excretion of Free and Protein-Bound Hemoglobin*†

Plasma Hemoglobin Concentration in Umbilical Cord Blood

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