Studies on lipo-protein cenapses of horse serum

Macheboeuf, M; Rebeyrotte, P

doi:10.1039/df9490600062

Cited by 29 publications

(8 citation statements)

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“…Studies on the human adult serum lipid transport system have established that the major serum lipids (triacylglycerol, cholesterol, cholesteryl esters, and phospholipids) are bound to particular protein constituents (14,32). designated apolipoproteins.…”

Section: Speculationmentioning

confidence: 99%

Studies on the Apolipoproteins and Lipoproteins of Cord Serum

McConathy

Lake

1980

Pediatr Res

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SummaryStudies on the cord serum lipid transport system were initiated to determine whether there is a correlation between decreased cord serum lipid levels and the absence or diminished level of some or all of the human serum apolipoproteins. Immunologic studies indicated the presence of all the well-characterized apolipoproteins and provided evidence that these apolipoproteins occurred primarily as distinct lipoprotein species with a paucity of association complexes or what others have termed "triglyceride-rich" lipoproteins. Quantitation of the apolipoproteins present in cord serum by electroimmunoassay yielded the following mean levels: A-I = 730 mg/liter; A-11 = 410 &liter; apolipoprotein B = 280 mg/ liter; C-I = 59 mg/liter; C-I1 = 32 &liter; C-111 = 65 mg/liter; apolipoprotein D = 37 &liter; and apolipoprotein E = 85 mg/ liter. Levels of C-I, C-11, and apolipoprotein E approached adult levels (83 to 86% of the adult levels), whereas apolipoproteins B and D were most reduced when compared to the adult concentrations, 29 and 37%, respectively. The three other apolipoproteins were present at approximately one-half the levels found in adults. SpeculationThe immunochemical studies on the apolipoprotein levels and lipoprotein forms of cord serum provide part of the data necessary for studying the progressive changes in the human lipid transport system from its fetal form to that of the adult.Studies on the human adult serum lipid transport system have established that the major serum lipids (triacylglycerol, cholesterol, cholesteryl esters, and phospholipids) are bound to particular protein constituents (14, 32). designated apolipoproteins. Such lipid-protein complexes (lipoproteins) have been most commonly classified on the basis of two of their characteristic physical properties. i.e., hydrated density (26) and charge (30).Studies on the antigenic components of the major lipoprotein density classes and electrophoretic bands in the human adult have clearly demonstrated their protein heterogeneity (4, 37) and lead to a classification system based on apolipoproteins as the only distinct chemical markers of this system (1, 2). This concept has been developed into the lipoprotein family theory and has been described elsewhere (2). Recently, the levels of all well-recognized apolipoproteins have been reported (3).Application of these physicochemical techniques to cord sera has established that compared to normal adult levels, very low density lipoprotein (VLDL) is virtually absent (39) or present in low concentrations (13, 15), low-density lipoprotein (LDL) is markedly decreased (8,42), and the predominant lipoprotein density class is high-density lipoprotein (49). In addition, the lipid levels of cord sera are also lower than the corresponding levels in adult sera (42,49,50). However, it has not been established whether there is a correlation between the decreased cord serum lipid levels (42,49,50) and the absence or diminished level of some or all of the apolipoproteins. The studies described herein are the first...

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Section: Speculationmentioning

confidence: 99%

Studies on the Apolipoproteins and Lipoproteins of Cord Serum

McConathy

Lake

1980

Pediatr Res

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“…Preparation of Horse Serum Fraction.--Since the substrate of the enzyme appeared to be the al-lipoprotein, a fraction of horse serum was prepared following the method of Macheboeuf (16). However, the serum used was several months old and the material appeared to become denatured before complete purification was obtained.…”

Section: Studies Of the Action Of The Enzyme On Horse Serum Fractionsmentioning

confidence: 99%

Studies on a Lipoproteinase of Group a Streptococci

Krumwiede

1954

Journal of Experimental Medicine

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A streptococcal enzyme which causes opalescence in serum was described by Ward and Rudd in 1938. These authors found that the enzyme was produced by many types of group A streptococci, but not by streptococci belonging to other groups. Seitz filtrates of serum broth cultures of active strains produced opalescence in rabbit, mouse, or human sera. These authors postulated that the enzyme altered serum protein but found no evidence to substantiate their theory (1).The studies reported in this paper were undertaken to determine the nature of the alteration in serum responsible for the development of opalescence. I t was found that streptococci produce an enzyme, designated a lipoproteinase, which acts upon txrlipoproteins and splits them into lipid and protein moieties. Methods and MaterialsPaper E/ec~opbore~/s.--Electrophoretic patterns were prepared by a modification of the method described by Kunkel and Tiselius (2) using a buffer consisting of 9.83 gin. of sodium barbital and 6.5 gin. of sodium acetate per liter, adjusted to pH 8.8 with HCI (3). A double thickness of Whatman 1 filter paper was used for all patterns. When dectrophore~s was completed the papers were dried at 90-100°C. The upper sheet was stained with Sudan black to show the lipids (3), the lower with an alcoholic solution of bromphenol blue to show the proteins (2).Sudan Black Stain.--1.5 gm. of Sudan black B was suspended in 100 ml. of 70 per cent alcohol. After standing for several days the solution was filtered to remove any undissolved dye and diluted 1-1 with 70 per cent alcohol before use. The dried patterns were immersed in this solution for 15 minutes and then differentiated in 50 per cent alcohol. No attempt was made to remove all stain from the paper.Chem/ca/Ana/ysss.--Non-protein nitrogen was determined by the method of Koch and McMeekin described in reference 4, phosphorus by the method of Fiske and Subbarow described in reference 4, total lipids by the method of Bragdon (5), cholesterol bythe method of Bloor (6)(7). A micro Kjeldahl method was used for total nitrogen determination (8). A n~nhydrin method was employed to detect protein breakdown (9). Carotenes were determined by the method of Lewis, Bedan~lry, and H~g (I0). The protein content of enzyme

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“…3MM, moistened with 20 mm-citrate buffer, pH 3-5. The paper was inserted in a rheo-ionophoretic apparatus, which is a hanging-strip electrophoresis apparatus (Macheboeuf, Rebeyrotte & Brunerie, 1951; Williams, Pickels & Durrum, 1955). Rheo-ionophoresis was carried out at an applied voltage of 750v (14-1 v/cm.…”

Section: Control Ratsmentioning

confidence: 99%