The determination of haptoglobins in normal human serum

Smith, Harold H.; Owen, James

doi:10.1042/bj0780723

Cited by 32 publications

(9 citation statements)

References 16 publications

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“…of 8 to 154 mg./100 ml. This agrees reasonably weil with the series of 152 normals studied by Smith and Owen (1961), which gave a mean value of 93 mg./100 ml. with a range (mean ± S.D.)…”

Section: Methodssupporting

confidence: 91%

“…Haptoglobin was estimated by adding standard methaemoglobin solution to serum and determining the peroxidase activity of the resulting methaemoglobin complex colorimetrically (Owen, Better, and Hoban, 1960 This agrees reasonably weil with the series of 152 normals studied by Smith and Owen (1961), which gave a mean value of 93 mg./100 ml. with a range (mean ± S.D.)…”

Section: Methodssupporting

confidence: 63%

See 1 more Smart Citation

Serum haptoglobin in liver disease

Williams¹,

Speyer²,

Billing³

1961

Gut

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“…of 8 to 154 mg./100 ml. This agrees reasonably weil with the series of 152 normals studied by Smith and Owen (1961), which gave a mean value of 93 mg./100 ml. with a range (mean ± S.D.)…”

Section: Methodssupporting

confidence: 91%

Section: Methodssupporting

confidence: 63%

Serum haptoglobin in liver disease

Williams¹,

Speyer²,

Billing³

1961

Gut

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“…The transverse tubules are opposite the lateral regions of the A band. In view of the fact that each transverse tubule is associated with a cisterna of the sarcoplasmic reticulum, it is referred to as a "dyad" (10). Occasionally, the transverse tubules branch and then associate with the sarcoplasmic reticulum.…”

Section: Observationsmentioning

confidence: 99%

THE MYOFILAMENT ARRANGEMENT IN THE FEMORAL MUSCLE OF THE COCKROACH, LEUCOPHAEA MADERAE FABRICIUS

Hagopian

1966

The Journal of Cell Biology

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The structure of the femoral muscle of the cockroach, Leucophaea maderae, was investigated by light and electron microscopy. The several hundred fibers of either the extensor or flexor muscle are 20 to 40 # in diameter in transverse sections and are subdivided into closely packed myofibrils. In glutaraldehyde-fixed and epoxy resin-embedded material of stretched fibers, the A band is about 4.5 # long, the thin filaments are about 2.3/z in length, the H zone and I band vary with the amount of stretch, and the M band is absent. The transverse sections of the filaments reveal in the area of a single overlap of thick and thin filaments an array of 10 to 12 thin filaments encircling each thick filament; whereas, in the area of double overlap in which the thin filaments interdigitate from opposite ends of the A band, the thin filaments show a twofold increase in number. The thick filament is approximately 205 to 185 A in diameter along most of its length, but at about 0.2 tz from the end it tapers to a point. Furthermore, some well oriented, very thin transverse sections show these filaments to have electron-transparent cores. The diameter of the thin filament is about 70 A. Transverse sections exhibit the sarcolemma invaginating clearly at regular intervals into the lateral regions of the A band. Three distinct types of mitochondria are associated with the muscle: an oval, an elongate, and a type with three processes. It is evident, in this muscle, that the sliding filament hypothesis is valid, and that perhaps the function of the extra thin filaments is to increase the tensile strength of the fiber and to create additional reactive rites between the thick and thin filaments. These sites are probably required for the functioning of the long sarcomeres.

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“…)< 1600. skeletal muscle, which appears in a constant relation to the cross-striated pattern of the myofibrils in longitudinal sections, dates back more than half a century (78). The fine reticular staining pattern in the sarcoplasm of muscle fibers which has been obtained by the application of our L D H method to the white adductor magnus muscle of the rabbit corresponds in many of its features to the descriptions of Veratti (79) who used a modification of Golgi's silver impregnation method.…”

Section: The Role Of Nadi-i-diaphorasementioning

confidence: 99%

Cytochemical Localization of Lactic Dehydrogenase in White Skeletal Muscle

Fahimi

Amarasingham

1964

The Journal of Cell Biology

123

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The limitations of the conventional histochemical methods for localization of lactic dehydrogcnasc (LDH) in white skeletal musclc have becn analyzed quantitatively. It is demonstrated that more than 80 per cent of LDH diffuses into the incubation medium within the first l0 minutes of incubation. Furthermore, it is confirmcd that the addition of phenazine methosulfatc (PMS) to the ingredients of the histochemical reaction for LDH increases substantially the capacity of the whitc muscle extract to reduce Nitro-BT. Based on these observations, a modified method of cytochcmical localization of LDH has been developed. This method prevents the leakage of LDH from tissue sections by thc application of all the ingredients of the histochcmical reaction to tissue sections in a thin gelatin film. The incubation mixture contains PMS so that the staining system is independent of tissue diaphorase. The application of this method to the adductor magnus muscle of the rabbit rcvcaled a fine rcticulum in the sarcoplasm of all muscle fibers, in addition to the staining of mitochondria. The distribution of the staining suggcsts that LDH is localizcd in the sarcoplasmic reticulum.

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The determination of haptoglobins in normal human serum

Cited by 32 publications

References 16 publications

Serum haptoglobin in liver disease

Serum haptoglobin in liver disease

THE MYOFILAMENT ARRANGEMENT IN THE FEMORAL MUSCLE OF THE COCKROACH, LEUCOPHAEA MADERAE FABRICIUS

Cytochemical Localization of Lactic Dehydrogenase in White Skeletal Muscle

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